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stringlengths 6
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B1HVP6 | MFEKPLGMRDTFPQIFEKVEAVRQTGRDFLTKRGYEFIKTPAVEYFDTVGKASAIADTHLFKLVDSQGNTLVLRPDMTTPIARVATSKLLKEMIPQRLAYFASVFRAQEAEGGRPAEFDQMGIELIGDQSVFADAEVIVTAMELLKHLKLEAFKVTIGHAGILNCILQDYTESIEQQTTLRTLLVHRNYVGFEEAVDSFNLPKAKADALLQFIEEAMDVKDIRDIEKYVRKNDALVYMQQLAQLLEMADLAAYVTFDFTLSSHMSYYTGMLFEVFALGSGFPLGNGGRYDGLLEVFGSKAGATGFSIRVDRLLETLHGQSEMQQEATVVLFDEEQFEAALIKVNTLRAAGKLATLQLRSSLVDEEAFLAHFTEVVVVGQEEIGSE | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 42992
Sequence Length: 385
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
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Q2W2D0 | MTESANRALLPAGLRDMLPPDAEFEASVVHSLMSMFARHGYDRVKPPLIEFEESLLDGAGGGTSSQTFRVMDPMSQKMMGLRADMTPQVARIAATRLGSQPRPLRLSYAGQVLRVKGTQLRPERQFGQAGIELIGSDDAGADAEVLVMTAEALDDLGVPGVSADLALPTLVPAVFAAYGINGETADRLRAALDHKDSATVAAQGGAAAPLLQALIAAAGPAARALAELCALDLPPAAAAERDRLARVVELAGADLPSLTLTVDPVENRGFEYHTGLSFTLFARNMGAELGRGGRYQGGGGEPATGATLFMDSVLAALPGPKPAKRLFVPAGTPRAWAQAFRAQGWVTVSGLDPAADPQVEAKHQGCRHRLGPDGIVEVE | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 39612
Sequence Length: 379
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
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A6VYL1 | MTLADRWLLPEGVDEALPEQAAKIEHLRRTLLNLHESWGYHLVIPPLLEYLDSLLTGAGSDLEIETFKVIDQLSGRLLGIRADFTSQVARIDAHCLKDDGVQRLSYCGSVLRTMPAGLDGTRSPIQLGAEIYGHGGVESDVEVLSLMLQTLSTAGLSNLVLDLGHVDIVSGVLAACNLNADQESKLIELYKAKDLPELDRYAEELGCLTDIQKQWLVGLPRLCGGKEVLKHATDLLGDVNESIRDAIVLLQKVSDSICQRFPKVGLHFDLSDLVSYSYHTGVIFAAYVPGHGNAIARGGRYNNIGQVFGRSRPATGFSTDVKALVALTDIVVNKPKTVLSPICSSDELWQKANSLRAEGYRVVEVLDDICAGDADFKLEFVDEAWQLMPVHN | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 42886
Sequence Length: 392
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
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Q2RGV6 | MASNLPLQLPAGVSDLLPPEAAALRQLEQRLLNCFRSWGYQEVMTPTFEFATTFQAGSPAGEEGALYKFIDRQGRVLALRPEMTAPIARLVATSLRRRELPLRLGYSARVFRYEEPQAGRRREFHQAGVELIGAGGVAGDVEIIALAVESLAQAGLEDFRLGLGQVAVTKGVLQDLALPPEAVAGIKSALASKDLVALERIYDEYHLEGERRRRLELLATIHGGREALEEARACFGRTAAAASLAELSRVWEALGAAGLEKWLFIDLGILRDFDYYTGIVFEGYVPGLGAPVCGGGRYDGLLAQFGYPCPATGFALGLERLLLARGETAPASLAGGYLVAGRDLAALLKRARELRSKGTAVVLDGESRSRQEAAARAAARGLNLEWIGE | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 41904
Sequence Length: 389
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
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Q9K013 | MQTWQLPEHIADVLPTNARQLESAREQLLALFRVHGYELVQPPLMEYAHSLLTHIDAGLSLKTILVTDRLSGRQLGIRADITPQVARIDAHLLSANQGINRLCYAGPVLHAQPDGLLNMREPLQAGAEMYGFADIRGDIELIDLMLKSMKIADMGKVLLSLGHIGIFRALSDAAHLDAGQSATLLALMQDKDTGAVEAQVKAWKLDGMWAKAFSLLPRLYGGREVLSDARGRLPDLSAVGGALGELQAVCDAFPDCEIHIDLSELRVDNYHTGLLYAAYAADFHDAVARGGRYDGLGGYFGRARPATGFSFDLRSFIGRLPAIERQPAVLVDAEDAEAAHEAVEALREQGQCVVIDYGIGHNVSEELAGRLKKTDGVWQVVKR | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity).
Sequence Mass (Da): 41746
Sequence Length: 383
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
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Q82V28 | MRNWLLPEYIEDVLPRDAYRIEKIRRLIMDMLFAHGYQFVMPPLLEYVESLLAGSGSGMNLRMFKVVDQLSGRMMGLRADMTPQAARIDAHLLNISGVTRLCYASSVVHTVPDEITRTREPFQVGAELYGHSGIESDLEIQCLLLECLSVSGIHSIHLDLGHIRVFRSLIRDSGIKPEFEMELYAALWAKDISSLKELVRTGLNKRLTRSVQNALLLLPELYGDGTVLLSARQHLPDFPEIGEALDQLEHVARILQPYVDRITFDLADLRGYHYHTGMVFAVYTPGCPAPIALGGRYDEIGKSFGRARPATGFSLDLKQLSQLTDMNGYPSGILAPWKPEDEKLAAMVRQLRAEGHIVVTELPGEENQEVTGCDRKLVFRNGNWEIDPVTG | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 43900
Sequence Length: 391
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
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Q2YBX1 | MNMSAWALPEYIEDILPAEALKIEMMRRRVLDWLFVNGYELVGPPLLEYVESLLTGSGGQMNLRVLKVVDQLSGRMMGLRADMTPQVARIDAHLLNRKGITRLCYAGSVLHARPSGLTRTREPLQIGAELYGHQGLESDLEIQRLMLQSLAIAGVGNIHLDLGHVAVFRGLIRSTGISPDLEMELSGALQGKDKAALKELCAGLKKQVDASVREALQLLPELYGDENVLTLARSALPSYPGIMKALDELEMVASELSPLVDTLAFDLADLRGYHYHSGMVFAAYTDNCPNAIAVGGRYDEVGKAFGRARPATGFSMDLRELSGLMSSDSHPRGILAPFIKEDKALEKKIEQLRNEGQIVIVALPGHENDAGSFNCDKKLVSENGVWSIADALI | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 42932
Sequence Length: 393
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
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Q97YX6 | MNRDIGKNAERELVSILRGEGFNAVRIPTSNSSPNPLPDIFATKGNTLLSIECKSTWENKVKVKEHQVRKLLDFLSMFTMKGVPLIAIKFKQVHEWRVLVPEKAEDIIVTIDNSIPIEDLFKILEKRIEEKILTP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Acts only on 4-way DNA junctions in a sequence non-specific manner; introduces paired nicks in opposing strands 2 bases 3' of the point of strand exchange only on continuous strands of 4-way junction DNA. Cleaves both mobile and immobile junctions.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 15452
Sequence Length: 135
EC: 3.1.21.10
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O07778 | MPITPLLHESVARFAATGADITTRAEPDLFVSIDPDHLRRILTAVLDNAITHGDGEIAVTAHARDGAVDIGVRDHGPGFADHFLPVAFDRFTRADTARGGRGSGLGLAIVAALTTTHGGHANATNHPDGGAELRITLPTPRPPFHEELPRITSSDTKDPNREHDTSDQ | Function: Member of the three-protein two-component system HK1/HK2/TcrA. Kinase that binds ATP and catalyzes the transfer of a phosphoryl group from ATP to HK2.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 17854
Sequence Length: 168
EC: 2.7.13.3
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O07777 | MALVLAAAGAVTVVQFRDAAHEADPDGALRGLTDDITADLVRELVTILPIVLVIAAVAAYLLSRAALRPVDRIRAAAQTLTTTPHPDTDAPLPVPPTDDEIAWLATTLNTMLTRLQRALAHEQQFVADASHELRTPLALLTTELELRCAGPDPPTS | Function: Member of the three-protein two-component system HK1/HK2/TcrA. HK2 transfers its phosphoryl group to TcrA.
PTM: Phosphorylated by HK1.
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 16595
Sequence Length: 156
Subcellular Location: Cell membrane
EC: 2.7.13.3
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Q91W97 | MFAVHLVAFYFTKLKEDQIKKVDRFLYHMRLSDETLVDIMARFQAEMEKGLGKDTNPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQEGQQNVQMESQFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRLATAMKKHKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGDEGRMCINTEWGAFGDDGALEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAMEMSKEGLANTREILVDLGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILTRLRENKKLARLRTTVGMDGTLYKTHPQYPKRLHKVVRRLVPNCDVRFLLSESGSTKGAAMVTAVASRVQAQRKQIDKVLALFQLTREQLLGVRDKMRAELEYGLKKKTHSLATVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKIRRRSVRMYNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDMLREAIKRRNEFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVDGDEGRMCVNTEWGGFGDNGCIDDIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESDRLALLQVRRILQQLGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLQHFKVTVGVDGTLYKLHPHFSRILQETVKELAPQCDVTFMLSEDGSGKGAALITAVAKRLQQPRKDI | Function: Catalyzes the phosphorylation of hexose to hexose 6-phosphate, although at very low level compared to other hexokinases (By similarity). Has low glucose phosphorylating activity compared to other hexokinases (By similarity). Involved in glucose homeostasis and hepatic lipid accumulation . Required to maintain whole-body glucose homeostasis during pregnancy; however additional evidences are required to confirm this role .
Catalytic Activity: ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 102259
Sequence Length: 915
Pathway: Carbohydrate metabolism; hexose metabolism.
Subcellular Location: Cytoplasm
EC: 2.7.1.1
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P0DUM0 | MLSKYQPSAHIAVTRAHWEDLHQAISSGKVTIDGNSLTLADVVAVSKFGCYARLSENRETIDAINESVSTLQECLDEGHHIYGVNTGFGGSADSRTDHLASLQRALLQLLQSGILTKADIGSGDTPSQSHAMPPEWVKAIMVVRSNSVARGHSAVSIGSIEAILRLLQRDITPVVPLRGTISASGDLMPLAYIVGAIEGNPGVFARAGKSPHGQALPAQQVLEQLGIPRITLGPKEALGLVNGTAASAALSSLVLYEAHRLALLSQVTTALTVEALRGSAESFHPFISQARPHDGQMEAASNILTVMRGSRLAMGTSEVQTGLVQDRYSLRTASQWIGPQLEDLLLADRQITVELNSTTDNPLIDSVSRHFYCGGNFQATSVTSAMEKTRLALQMLGKLMFAQCSEMIDPSLNNGLPTNLVADDPSLSFTMKGVDISMAAYMSELAYLANPVSSHVQTAEMHNQAVNSLAFVSARYTMQAVDIVSMMSACSLYVACQALDLRVLQLNFFRELHPIVCNGTHDAFHTILAPKELERITQQLVTAIQDAWLTTSRMDAGDRCQRVIKLSLPILLNEMRGAIPSDRQQVDLLTSIGNWEEATCYKMLEAYKQTHERFCRTQNTVEYLGAGSKAIYHAIRHKVGVPFHQGFVEQPSADDLDTTAIINGREKKTTGGWISLIYEALRDDSLTGVILEAVQPVRSI | Function: Phenylalanine ammonia-lyase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines . The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockiamide A (Probable). Xenocockiamide A is then converted to hancockiamide D via a series of hydroxylations and O-methylations (Probable). The tyrosinase hkm6 may catalyze an aromatic hydroxylation, then the 2-oxoglutarate-dependent Fe(II) dioxygenase hkm4 and the FAD-dependent phenol hydroxylase hkm7 may catalyze consecutive hydroxylations to install 2 more hydroxy groups, and the methyltransferase hkm8 probably catalyzes two methylations using 2 molecules of S-adenosyl-L-methionine (SAM) (Probable). The NRPS hkm11 activates and transfers trans-cinnamate supplied by the PAL hkm12 to hancockiamide D and produces hancockiamide A . NRPS Hkm11 has the flexibility to tolerate the bulky hancockiamide G as a substrate and the absence of the acetyl-transferase hkm3 opens up the opportunity for hkm11 to introduce a second N-cinnamoyl moiety . The cytochrome P450 monooxygenase hkm5 catalyzes the methylenedioxy bridge formation, converting hancockiamide A into hancockiamide G . Hkm5 can also convert hancockiamide B into hancockiamide C, and hancockiamide D into hancockiamide H . The N-acetyltransferase hkm3 finally transfers an acetyl group to 1-N of piperazine, converting hancockiamide A into hancockiamide B and hancockiamide G into hancockiamide C .
PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Catalytic Activity: L-phenylalanine = (E)-cinnamate + NH4(+)
Sequence Mass (Da): 75940
Sequence Length: 700
Pathway: Secondary metabolite biosynthesis.
EC: 4.3.1.24
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P0DUL1 | MTKLDSPQFEPFELTAADYAFPMFYAGCTLSFRLKSPEMGIPVLQTAVERITAHLPFLTGIVIPSAVKDGVMEVHPAACGQSGLEDPQCRVRRLPHLCLPPKTASASANKKHGSGMTYDRNECLIVAPLEAATAAQQHPVIRFQINVLADGIIFTLFANHMVIDGTGLGIITEMLASCCQTADNTGSVPELAGAIDREARTRAMLGTIGRREREKVQFEPVAAESAAPDGHQEVHDASLVDCNFRLSADKIRRIRERAQELGIASASEDDIVTAVLWLCMSEFRSHSGAGKEISACTLLRMVNVRRRFHPAVPDNYLGNCYIMIEETLPTTDLSGGAAQASTEEDFLRLIGVVASVLRSRLNRVDDQYVRDHLAQFTHAGDWAHTTIHEPDVAVTSLRGMSVYSLDFGSVLSGIVDFETLPYMNPDGVCTIKPRRVIDPSWEVAVTLSREDMDRLRKNELFRWLVVGESYLHIFQSAQQVTTFA | Function: O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines . The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockiamide A (Probable). Xenocockiamide A is then converted to hancockiamide D via a series of hydroxylations and O-methylations (Probable). The tyrosinase hkm6 may catalyze an aromatic hydroxylation, then the 2-oxoglutarate-dependent Fe(II) dioxygenase hkm4 and the FAD-dependent phenol hydroxylase hkm7 may catalyze consecutive hydroxylations to install 2 more hydroxy groups, and the methyltransferase hkm8 probably catalyzes two methylations using 2 molecules of S-adenosyl-L-methionine (SAM) (Probable). The NRPS hkm11 activates and transfers trans-cinnamate supplied by the PAL hkm12 to hancockiamide D and produces hancockiamide A . NRPS Hkm11 has the flexibility to tolerate the bulky hancockiamide G as a substrate and the absence of the acetyl-transferase hkm3 opens up the opportunity for hkm11 to introduce a second N-cinnamoyl moiety . The cytochrome P450 monooxygenase hkm5 catalyzes the methylenedioxy bridge formation, converting hancockiamide A into hancockiamide G . Hkm5 can also convert hancockiamide B into hancockiamide C, and hancockiamide D into hancockiamide H . The N-acetyltransferase hkm3 finally transfers an acetyl group to 1-N of piperazine, converting hancockiamide A into hancockiamide B and hancockiamide G into hancockiamide C .
Sequence Mass (Da): 53302
Sequence Length: 484
Pathway: Secondary metabolite biosynthesis.
EC: 2.3.1.-
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P0DUL3 | METPTPPLPSKDQLFPPLIQLVRALLWVLVITIGGAIVQRLFFHPLRKIPGPLTAAISGWDEFYHNIWRDGEWCKTYPKLHKEYNSPVIRIGPNHVHLNDIDAYETVFRVGTNFYKDKTFYTCADNDGSIFSLCDRDEHSERRKVLSSLFSKQAAEMTAPKVMSKLNELLDFMITQSKEGKACNITDLFRALAINWVADTLLGDCGDVVTYAETKPDLLEDIDGLSKLIPTLRFFPYLIPTLNSLAPSTSPAGVAKFKKICENYTRPRINDPIKNISQRSRASVVELLIAHRHEVYHKPPTVDYLAEEAFTFIDAGVDTTGGTLVAAIYHILRDPGILRRLREELDESQLFLSKGTPIDFKKLGNLPYLNAVINESHRIWPALPGPLPRVVPPEGLQVGSFFVPSGTILSSTHHCLHYNETVFPEPKKFKPERWLRTDKWEGDRYLNPYSRGSRACIGINLAQMELRLTLGHLFSHYDLQLCEPTLSSLEWKDHFVAHPKAPVMIHIGFRKA | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines . The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockiamide A (Probable). Xenocockiamide A is then converted to hancockiamide D via a series of hydroxylations and O-methylations (Probable). The tyrosinase hkm6 may catalyze an aromatic hydroxylation, then the 2-oxoglutarate-dependent Fe(II) dioxygenase hkm4 and the FAD-dependent phenol hydroxylase hkm7 may catalyze consecutive hydroxylations to install 2 more hydroxy groups, and the methyltransferase hkm8 probably catalyzes two methylations using 2 molecules of S-adenosyl-L-methionine (SAM) (Probable). The NRPS hkm11 activates and transfers trans-cinnamate supplied by the PAL hkm12 to hancockiamide D and produces hancockiamide A . NRPS Hkm11 has the flexibility to tolerate the bulky hancockiamide G as a substrate and the absence of the acetyl-transferase hkm3 opens up the opportunity for hkm11 to introduce a second N-cinnamoyl moiety . The cytochrome P450 monooxygenase hkm5 catalyzes the methylenedioxy bridge formation, converting hancockiamide A into hancockiamide G . Hkm5 can also convert hancockiamide B into hancockiamide C, and hancockiamide D into hancockiamide H . The N-acetyltransferase hkm3 finally transfers an acetyl group to 1-N of piperazine, converting hancockiamide A into hancockiamide B and hancockiamide G into hancockiamide C .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58106
Sequence Length: 512
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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P0DUQ0 | MDDFSATHINYTLSIHLSGIFFAWHRHFVWLWERTLREECGYNGYQPYWDWALSANNISASPIFDGSPTSLSGNGDPINQEPFLQLEPTNITIPTGTGGGCVTNGPFANMTLNLPDLSMAGDEEFPSNAFDYKPHCFTRNLNSHMSSAFTSQADVDRLLNSPSITDLQANIDFSAWPELREARILGPHAAAHMSLGRTMDDFWTAPQDPSFMLHHAQVDRIWSLWQARGPESRRWALNGTSTINNRPTSPEVTLDTELVWGSLSESKTMREVMSTEAYHFCYEYGA | Cofactor: Binds 2 copper ions per subunit.
Function: Oxidase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines . The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockiamide A (Probable). Xenocockiamide A is then converted to hancockiamide D via a series of hydroxylations and O-methylations (Probable). The tyrosinase hkm6 may catalyze an aromatic hydroxylation, then the 2-oxoglutarate-dependent Fe(II) dioxygenase hkm4 and the FAD-dependent phenol hydroxylase hkm7 may catalyze consecutive hydroxylations to install 2 more hydroxy groups, and the methyltransferase hkm8 probably catalyzes two methylations using 2 molecules of S-adenosyl-L-methionine (SAM) (Probable). The NRPS hkm11 activates and transfers trans-cinnamate supplied by the PAL hkm12 to hancockiamide D and produces hancockiamide A . NRPS Hkm11 has the flexibility to tolerate the bulky hancockiamide G as a substrate and the absence of the acetyl-transferase hkm3 opens up the opportunity for hkm11 to introduce a second N-cinnamoyl moiety . The cytochrome P450 monooxygenase hkm5 catalyzes the methylenedioxy bridge formation, converting hancockiamide A into hancockiamide G . Hkm5 can also convert hancockiamide B into hancockiamide C, and hancockiamide D into hancockiamide H . The N-acetyltransferase hkm3 finally transfers an acetyl group to 1-N of piperazine, converting hancockiamide A into hancockiamide B and hancockiamide G into hancockiamide C .
Sequence Mass (Da): 32205
Sequence Length: 286
Pathway: Secondary metabolite biosynthesis.
EC: 1.14.-.-
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P0DUL5 | MEIFESFGIEGEVTKQWEPATDEILWCRNESGTLSRMERFRNEPPVGVKWTHGTLQQGRVEEIMKKRITEISGVEVEYSTELSDLTINTRESSNSKASACSVTIRSVADDQEAHRSSETIRARYIIGADGGRSSIRDLMGVAMEGTKGTAIWGVMDILGGSDFPDFGATSVVRSDSDGAVDFVRREEGLTRIYVELNKCAAGWEALERDTITPELILEKCRYIIRPYKLEVDYVEWWSSFTVWQRLSKSMIVHDRVFLVGDAVHTHSPLCGMGMNTGIQDSFNLGWKLAGVVQGQLNYDILQTYETERRPVAEALLDTDRTVLDLFHAPLGPEAEALLAKVPALQVYLGGRGICYHESVLTCRLAQTLGDLTAGECLPDVTVFDYATGRPSSTHSWIKGNGGWAIIVWAGDVSRPSQMNLVQSLSRDMIELRDSLGKSGSMIDFFLIHCSAWPSVELADFPPLFFPTTKTIGRPNGRIFVDEKAVYDGLHISRAEGGVAIVRPDKHIAWAGGLQEVDSLQRYLRQVFRPQPE | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines . The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockiamide A (Probable). Xenocockiamide A is then converted to hancockiamide D via a series of hydroxylations and O-methylations (Probable). The tyrosinase hkm6 may catalyze an aromatic hydroxylation, then the 2-oxoglutarate-dependent Fe(II) dioxygenase hkm4 and the FAD-dependent phenol hydroxylase hkm7 may catalyze consecutive hydroxylations to install 2 more hydroxy groups, and the methyltransferase hkm8 probably catalyzes two methylations using 2 molecules of S-adenosyl-L-methionine (SAM) (Probable). The NRPS hkm11 activates and transfers trans-cinnamate supplied by the PAL hkm12 to hancockiamide D and produces hancockiamide A . NRPS Hkm11 has the flexibility to tolerate the bulky hancockiamide G as a substrate and the absence of the acetyl-transferase hkm3 opens up the opportunity for hkm11 to introduce a second N-cinnamoyl moiety . The cytochrome P450 monooxygenase hkm5 catalyzes the methylenedioxy bridge formation, converting hancockiamide A into hancockiamide G . Hkm5 can also convert hancockiamide B into hancockiamide C, and hancockiamide D into hancockiamide H . The N-acetyltransferase hkm3 finally transfers an acetyl group to 1-N of piperazine, converting hancockiamide A into hancockiamide B and hancockiamide G into hancockiamide C .
Sequence Mass (Da): 59262
Sequence Length: 532
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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P0DUL6 | MRDRCMLSFTKEQLTSVGEYCTLHSSPLPKSVEEQCRVTDERSQDEVVMAPSPAQCAWLMSFALASRPRRILELGTFTGVSTLAFYEGTRKTKAEIITVDMSEEYLQIAETAFRRHGATDRIQTIRGPCLEILPTITGEFDLIYIDAAEEEYEAYTRFVLDHKLLSAEGVMLVDDGTYIRWFYFFQANWWSVLLEGLVVDRSIVKEFPEEIQEPYLGIADQMNDFNRYARSDPRVEVTMIPLFNGVTQITWK | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines . The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockiamide A (Probable). Xenocockiamide A is then converted to hancockiamide D via a series of hydroxylations and O-methylations (Probable). The tyrosinase hkm6 may catalyze an aromatic hydroxylation, then the 2-oxoglutarate-dependent Fe(II) dioxygenase hkm4 and the FAD-dependent phenol hydroxylase hkm7 may catalyze consecutive hydroxylations to install 2 more hydroxy groups, and the methyltransferase hkm8 probably catalyzes two methylations using 2 molecules of S-adenosyl-L-methionine (SAM) (Probable). The NRPS hkm11 activates and transfers trans-cinnamate supplied by the PAL hkm12 to hancockiamide D and produces hancockiamide A . NRPS Hkm11 has the flexibility to tolerate the bulky hancockiamide G as a substrate and the absence of the acetyl-transferase hkm3 opens up the opportunity for hkm11 to introduce a second N-cinnamoyl moiety . The cytochrome P450 monooxygenase hkm5 catalyzes the methylenedioxy bridge formation, converting hancockiamide A into hancockiamide G . Hkm5 can also convert hancockiamide B into hancockiamide C, and hancockiamide D into hancockiamide H . The N-acetyltransferase hkm3 finally transfers an acetyl group to 1-N of piperazine, converting hancockiamide A into hancockiamide B and hancockiamide G into hancockiamide C .
Sequence Mass (Da): 29031
Sequence Length: 252
Pathway: Secondary metabolite biosynthesis.
EC: 2.1.1.-
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A5FVE7 | MAEHDDGDLIAAIRGLARANVLVVGDLMLDRYAYGRVERISPEAPVPILTVTREIAMPGGAGNVVRNLTALDAAAAFVSVVGDDQEGSDLTALIGGQPNVEPWLLVETGRATTVKTRYIAAGQHLIRADRELVMPLTDKLGERLLKIASDAMAATSVTVLSDYRKGVLAPTIARNLIASARSIGRTVIVDPKGADWSHYAEADVITPNRRELAEAVGRDLPDEAAIVGAAREVIGRFGFGAVLCTRSEDGMSLVTVDTVRHYPAEAAEVYDVSGAGDTVVAVLAAGLASGLPLEIAARLSNIAGGLVVGKVGTAVARPDDLVDAVKPASGALRKVVTRQAAAEAAERWRQRGWRIGFTNGCFDLLHPGHVHLLEQARAGCDRLVVGLNADSSVRRLKGATRPVQPEAARAAVLASLASVDLVVIFEEDTPLDLLSAIRPDVLVKGADYTHDTVVGAREVESWGGRVMLAELLPGHSTTATVTRLRS | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da): 51236
Sequence Length: 486
Pathway: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
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Q9Z5B5 | MTGPMAVRTDRTPLVVVGDALLDRDLTGTADRLAPDAPVPVVQECAERIRPGGAALAAYLAARDGREVTLIAGVGEDPAGLALRELLAPWLKLIPLPLTGTVPEKTRVLAQDRPVVRLDRGGGRVREATDEARDALGCARAVLVSDYGRGAADALRDVLAARPPLVWDPHPRGGPPVPGTRLVTPAEKEAHGFAPSEGRPGGGLRAAALNAAALVRDWRVAAVTVTLGSRGALLSYGEHPLLVPAPAAHHGDSCGAGDRFAATAAGLLADGALVGEAVEGAVGAATAFVAAGGAAAVPPAGSERALAALPDTDDPGALAARIRAEHGTVVAAGGCFDLLHAGHVGLLQAARRLGDCLVVCVNSDASVRRGKGGGRPVNPLADRVRVLRALACVDAVAVFDEDTPERLLGELRPDVWVKGGDYAGADLPEAGLLKEWGGQAVLLPYLDGRSSTALLARAAEGAR | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da): 47193
Sequence Length: 463
Pathway: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
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P41936 | MFNVSALRAATPSIASVSSVASPSEQHGLSTSVGVGVNDTTSRTGDGGAASSASSASAAPQQQSQSALHNKLEAKWDTLLPTDTNLQCSTWPDSIPLLAGYSATPTFSFDPCTYGSYDPSAYFASNGIAGSMYTLPDQFPRSENDMLDNSNTSNGNKSDKDGIKLEDEDEILEDEENDEEDDGTGKRKKRKRRVLFTKAQTYELERRFRSQKYLSAPEREALAMQIRLTPTQVKIWFQNHRYKTKKSHTDKPINAALLTTMPNAFSSQSTAASFPTRAMPIPMLVRDSSARSSDISSTSPYTVAFGSANSGYLPTPSAYLPATSGYFSNGPSAASSYMTNTQWWPS | Function: Involved in combinatorial activation of gene expression in pharyngeal muscle. Specifically binds a site necessary for activity of the B subelement of myo-2 enhancer.
Sequence Mass (Da): 37511
Sequence Length: 346
Domain: The homeobox domain is required for the induction of distal tip cell fate.
Subcellular Location: Nucleus
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P02836 | MALEDRCSPQSAPSPITLQMQHLHHQQQQQQQQQQQMQHLHQLQQLQQLHQQQLAAGVFHHPAMAFDAAAAAAAAAAAAAAHAHAAALQQRLSGSGSPASCSTPASSTPLTIKEEESDSVIGDMSFHNQTHTTNEEEEAEEDDDIDVDVDDTSAGGRLPPPAHQQQSTAKPSLAFSISNILSDRFGDVQKPGKSMENQASIFRPFEASRSQTATPSAFTRVDLLEFSRQQQAAAAAATAAMMLERANFLNCFNPAAYPRIHEEIVQSRLRRSAANAVIPPPMSSKMSDANPEKSALGSLCKAVSQIGQPAAPTMTQPPLSSSASSLASPPPASNASTISSTSSVATSSSSSSSGCSSAASSLNSSPSSRLGASGSGVNASSPQPQPIPPPSAVSRDSGMESSDDTRSETGSTTTEGGKNEMWPAWVYCTRYSDRPSSGPRYRRPKQPKDKTNDEKRPRTAFSSEQLARLKREFNENRYLTERRRQQLSSELGLNEAQIKIWFQNKRAKIKKSTGSKNPLALQLMAQGLYNHTTVPLTKEEEELEMRMNGQIP | Function: This protein specifies the body segmentation pattern. It is required for the development of the central nervous system. Transcriptional regulator that represses activated promoters. Wg signaling operates by inactivating the SGG repression of EN autoactivation.
PTM: Phosphorylated. Phosphorylation may directly or allosterically modify its function.
Sequence Mass (Da): 59411
Sequence Length: 552
Subcellular Location: Nucleus
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P23397 | QDEKRPRTAFTGDQLARLKREFSENKYLTEQRRTCLAKELNLNESQIKIWFQNKRAKMKKASGVKNQLALQLMAQGLYNHSSSSSSSSSSSSSIFLLA | Function: This protein specifies the body segmentation pattern.
PTM: Phosphorylated in the Ser-rich domain.
Sequence Mass (Da): 11143
Sequence Length: 98
Subcellular Location: Nucleus
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E4QP00 | MTDTIFDYVIVGGGTAGSVLANRLSARPENRVLLIEAGIDTPENNIPPEIHDGLRPWLPRLSGDKFFWPNLTIHRAAEHPGITREPQFYEQGRLLGGGSSVNMVVSNRGLPRDYDEWQALGADGWDWQGVLPYFIKTERDADYGDDPLHGNAGPIPIGRVDSRHWSDFTVAATQALEAAGLPNIHDQNARFDDGYFPPAFTLKGEERFSAARGYLDASVRVRPNLSLWTESRVLKLLTTGNAITGVSVLRGRETLQVQAREVILTAGALQSPAILLRTGIGPAADLHALGIPVLADRPGVGRNLWEHSSIGVVAPLTEQARADASTGKAGSRHQLGIRASSGVDPATPSDLFLHIGADPVSGLASAVFWVNKPSSTGWLKLKDADPFSYPDVDFNLLSDPRDLGRLKAGLRLITHYFAAPSLAKYGLALALSRFAAPQPGGPLLNDLLQDEAALERYLRTNVGGVWHASGTARIGRADDSQAVVDKAGRVYGVTGLRVADASIMPTVPTANTNLPTLMLAEKIADAILTQA | Function: Involved in the degradation and detoxification of 5-(hydroxymethyl)furfural (HMF) by mediating its oxidation to furan-2,5-dicarboxylate (FDCA), a biobased platform chemical for the production of polymers. Active with a wide range of aromatic and aliphatic primary alcohols and aldehydes: acts on alcohol groups and requires the spontaneous hydration of aldehyde groups for their oxidation . To a lesser extent, is also able to catalyze the oxidation of thiols that are structurally similar to its alcohol substrates, yielding the corresponding thiocarbonyls .
Catalytic Activity: 5-hydroxymethylfurfural + 2 H2O + 3 O2 = 2,5-dicarboxyfuran + 2 H(+) + 3 H2O2
Sequence Mass (Da): 57014
Sequence Length: 531
EC: 1.1.3.47
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P30519 | MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQCPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQAGSTLARETLEDGFPVHDGKGDMRKCPFYAAEQDKGALEGSSCPFRTAMAVLRKPSLQFILAAGVALAAGLLAWYYM | Function: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron.
PTM: A soluble form arises by proteolytic removal of the membrane anchor.
Location Topology: Single-pass type IV membrane protein
Catalytic Activity: heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Sequence Mass (Da): 36033
Sequence Length: 316
Subcellular Location: Microsome membrane
EC: 1.14.14.18
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P43242 | MSAEVETSEGVDEPEEKNFGENHIRMADLSELLKEGTKEAHDRAENTKFVKDFLKGNIKKEIFKLATTALYFTYSALEEEMDRNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQCSEAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFENVDNAQQFKQFYRARMNALDLNLKTKERIVEEANKAFEYNMQIFSELDQAGSAPASETVEDRIPVHDGKGDVRKCPYYAAGQVNGALEGSSCPFRAAMAVLRKPSLQLVLAAAVALAAGLLAWYYM | Function: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
Catalytic Activity: heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Sequence Mass (Da): 35373
Sequence Length: 312
Subcellular Location: Microsome
EC: 1.14.14.18
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P23711 | MSSEVETSEGVDESENNSTAPEKENHTKMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMDRNKDHPAFAPLYFPTELHRKEALIKDMEYFFGENWEEQVKCSEAAQKYVDRIHYVGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFEHVDNAQQFKQFYRARMNALDLSMKTKERIVEEANKAFEYNMQIFSELDQAGSMLTKETLEDGLPVHDGKGDVRKCPFYAAQPDKGTLGGSNCPFRTAMAVLRKPSLQLILAASVALVAGLLAWYYM | Function: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron.
PTM: A soluble form arises by proteolytic removal of the membrane anchor.
Location Topology: Single-pass type IV membrane protein
Catalytic Activity: heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Sequence Mass (Da): 35762
Sequence Length: 315
Subcellular Location: Microsome membrane
EC: 1.14.14.18
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Q9C9L4 | MATTRLNPSCHFPASTRLSCESYLGLRTTGRISYARTLTAPRGYLAVKANGGQASVVTAAAITEKQQKKYPGESKGFVEEMRFVAMRLHTKDQAREGEKESRSPEEGPVAKWEPTVEGYLHFLVDSKLVYDTLEGIIDGSNFPTYAGFKNTGLERAESLRKDLEWFKEQGYEIPEPMAPGKTYSEYLKDLAENDPQAFICHFYNIYFAHSAGGQMIGTKVSKKILDNKELEFYKWDGQLSQLLQNVRQKLNKVAEWWTREEKSHCLEETEKSFKFSGEILRLILS | Function: Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Plays a minor role in phytochrome assembly and photomorphogenesis.
Catalytic Activity: heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Sequence Mass (Da): 32434
Sequence Length: 285
Subcellular Location: Plastid
EC: 1.14.14.18
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O70453 | MSSEVETAEAVDESEKNSMASEKENHSKIADFSDLLKEGTKEADDRAENTQFVKDFLKGNIKKELFKLATTALSYSAPEEEMDSLTKDMEYFFGENWEEKVKCSEAAQTYVDQIHYVGQNEPEHLVAHTYSTYMGGNLSGDQVLKKETQPVPFTREGTQFYLFEHVDNAKQFKLFYCARLNALDLNLKTKERIVEEATKAFEYNMQIFSELDQAGSIPVRETLKNGLSILDGKGGVCKCPFNAAQPDKGTLGGSNCPFQMSMALLRKPNLQLILVASMALVAGLLAWYYM | Function: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Heme oxygenase 3 could be implicated in some heme-dependent regulatory role in the cell.
Catalytic Activity: heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Sequence Mass (Da): 32592
Sequence Length: 290
EC: 1.14.14.18
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Q9LQC0 | MATSRLNASCRFPASRRLDCESYVSLRAKTVTIRYVRTIAAPRRHLVRRANEDQTLVVNVVAAAGEKPERRYPREPNGFVEEMRFVVMKIHPRDQVKEGKSDSNDLVSTWNFTIEGYLKFLVDSKLVFETLERIINESAIQAYAGLKNTGLERAENLSRDLEWFKEQGYEIPESMVPGKAYSQYLKNIAEKDPPAFICHFYNINFAHSAGGRMIGTKVAEKILDNKELEFYKWDGQLSELLQNVSEELNKVAELWTREEKNHCLEETEKSFKFYWEIFRYLLS | Function: Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Plays a minor role in phytochrome assembly and photomorphogenesis.
Catalytic Activity: heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Sequence Mass (Da): 32953
Sequence Length: 283
Subcellular Location: Plastid
EC: 1.14.14.18
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O73688 | MEADKKTTAQTESNRDLSEQIKKVTKDVHVRAESTELMLSFQRGQVTLQQYKLLLCSLYEIYLALEEEMDRNCDHPSVAPIYFPAELARLATIEKDLEFFFGPDWREKIVVPAATERYCHRIRQIGQENPEYLIAHAYTRYLGDLSGGQVLGRIAQKSMKLGGSEGLSFFAFPGVSSPNLFKRLYRSRMNSVELTEEQRSAVLQEALGAFEFNIQVFEDLQKMLNVTENEPGVGTPRSRPATTLQVGGSMIQTNPLFRMVLGLCLALATVSIGLYAL | Function: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
Catalytic Activity: heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Sequence Mass (Da): 31211
Sequence Length: 277
Subcellular Location: Microsome
EC: 1.14.14.18
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O52792 | MTYVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRMLRDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVPYTICTLSSVSLEEIAAVGGRPWFQLYWLRDEKRSLDLVRRAEDAGCEAIVFTVDVPWMGRRLRDMRNGFALPEWVTAANFDAGTAAHRRTQGVSAVADHTAREFAPATWESVEAVRAHTDLPVVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVSGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQLLELLAEEVRDAMGLAGCESVGAARRLNTKLGVV | Function: Catalyzes the oxidation of p-hydroxymandelate to p-hydroxybenzoylformate in the biosynthesis of L-(4-hydroxyphenyl)glycine and L-(3,5-dihydroxyphenyl)glycine, 2 non-proteinogenic amino acids occurring in the vancomycin group of antibiotics.
Catalytic Activity: (S)-4-hydroxymandelate + O2 = 4-hydroxyphenylglyoxylate + H2O2
Sequence Mass (Da): 37832
Sequence Length: 357
Pathway: Antibiotic biosynthesis; vancomycin biosynthesis.
EC: 1.1.3.46
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Q8Y563 | MKKVFITTGTEHYLRQLMANYTGGNVTLLQNFSQSLLYQESTGEKLFQEGAEYRVLQSSGSIKGFGVVVFEYIHLRDEEIPIFLQMYQRASLHFSETPGLQSTKLTKAMNMNKFLIISFWDSEVFFHDWKKSPLSKEITNIMRKNNTQSGFSHEDIYHYPEFSHDAK | Function: Catalyzes the degradation of heme to biliverdin in the presence of a suitable electron donor such as ascorbate, with the subsequent release of iron. Hardly any CO is released by the heme degradation reaction. Binds heme . Allows bacterial pathogens to use the host heme as an iron source. Release of iron from heme may play a crucial role in the pathogenicity of L.monocytogenes (Probable).
Sequence Mass (Da): 19466
Sequence Length: 167
Subcellular Location: Cytoplasm
EC: 1.14.-.-
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Q988D0 | MRRKVFEELVTATKILLNEGIMDTFGHISARDPEDPASFFLAQKLAPSLITVDDIQRFNLDGETSDNRPSYLERYIHSEIYKTRPDVQCVLHTHSPAVLPYCFVDTPLRPVTHMGAFIGESVPVYEIRDKHGDETDLFGGSPDVCADIAESLGSQTVVLMARHGVVNVGKSVREVVFRAFYLEQEAAALTAGLKIGNVKYLSPGEIKTAGKLVGAQIDRGWNHWSQRLRQAGLA | Cofactor: Binds 1 manganese ion per subunit.
Function: Involved in the catabolism of pyridoxal 5-phosphate (Vitamin B6). Catalyzes the decarboxylation of 3-hydroxy-2-methylpyridine-4,5-dicarboxylate to yield 3-hydroxy-2-methylpyridine-5-carboxylate. The decarboxylation proceeds by an aldolase-like mechanism in which the binding of the substrate frees Glu-73 residue from its interaction with manganese ion replacing it by an interaction with the hydroxyl group from the substrate. Glu-73 residue then provides the proton for the keto-enol tautomerization. The decarboxylation reaction is analogous to the retroaldol reaction except that it does not need a base as the carboxylate is likely to be deprotonated under the reaction conditions.
Catalytic Activity: 5-hydroxy-6-methylpyridine-3,4-dicarboxylate + H(+) = 3-hydroxy-2-methylpyridine-5-carboxylate + CO2
Sequence Mass (Da): 25939
Sequence Length: 234
Pathway: Cofactor degradation; B6 vitamer degradation.
EC: 4.1.1.51
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Q88DY1 | MLQVEGLYLCRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVARSYLALSGGERQRVHLARVLAQLWPGEEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVYGIDVLVQAHPERGHPLIITR | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27656
Sequence Length: 255
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q3ICT8 | MLCANNVSAQIGQKKLLKHINFYVKPNELVVIIGPNGAGKSSLLKALCGDIKINNGDITLNDRLLSDYSIASLATLRAVLTQNYELDFPFSVAEVVDMAHFAHQADYSKQQLMHFSEQVMQALSVTHLKTHTFTQLSGGEKQRVQLARVLCQIQPSLVANKTPYLLIDEPTSSLDIFHQYDVMAQAKSIASQGAGVVAVIHDLSLAASFADRIYMLNNGEVAACGIPKEVLTPALLKRVYNINARLENNTSEAMPHIQMCY | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28686
Sequence Length: 261
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q1MCZ1 | MIEVSGVSVRLSGKTIISDVAFTARAGELTAIAGPNGSGKTTTMKAISGELAYGGSVRIGGGEVKGLKPWQLAAIRGVLPQASTISFPFTVREIVRMGLTSGLNLHPDKAEQTAAAALASVDLTGFEGRFYQELSGGEQQRVQLARVLCQIAEPIVDGKPCWLLLDEPVSSLDISHQLTIMTLARNFCERGGGVIAVMHDLNLTALFADRIVLMKSGRLAAAGSIGEVLTNETMLAVFGCALRINQVPSDGTPFVLAHSAISRP | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27743
Sequence Length: 264
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q98L75 | MIEARDVSVDIAGKRIVGGVDFDARPGEVAAIVGPNGSGKTTFLKALSGEFAYTGRIALNGHNLSSMRPAEMAVHRAVLPQATTLSFPFTVREVVKLGLVGGRSGALPGEDARLPERALARVDLDGFAGRFYQELSGGEQQRVQLARVLCQVWAPVLDGKPRYLFLDEPVSSLDIKHQLIIMNIARDFAKRGGGVVAILHDLNLTSMYADRIFVMHRGRLAATGSPQDVLSDDLIEKVFDCRLRVGVLPAGNMPFVLPQSSVY | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28452
Sequence Length: 263
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q0SIB7 | MSPAFHPLRTRVGEAIEQSLFRRTDPVPPPRPSGAVTLRADGIAVTRGGRPVLDDVSVDVRIGEVLVLVGPNGAGKSTLLAALSGDQDVHTGTVHLDDRDLGEWTALEMAQRRAVLPQQNTVGFSFTARQVITMGRSPWARTPRSDDDAVAIAEAMRICDVVAFADRPFTALSGGERARVALARVLAQRTETILLDEPTAALDLGHQETVMRLARSRAEQGTAVVVVLHDLALAAAYADRIVVLEQGRVAANGPPADVLSEELLTRVYGHPVEVIEHPVTGATLVLPRRDQR | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31376
Sequence Length: 292
Subcellular Location: Cell membrane
EC: 7.6.2.-
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Q160G4 | MSLDAADITVKLGRTPILHGIGFCAKPGEVSAIVGPNGSGKTTLLRAITGDLPFDGTVRLNGKDTSRMKPWELSAIRAVLPQSAVLAFPFTVAEVVRLGVQAGVCARDCDAPMAALSQVRLAHYADRFYHELSGGEQQRVQLARVLAQVWRPVVGGAPRWLLLDEPVASLDIANQLEVMEITRAYASAGGGVVAVMHDLNLTAMFADHLAILSGGQCLAAGPPEQVMTDAILSQAYGCALRVNTPPPHSATYVLPHAANRL | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27606
Sequence Length: 261
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q8EB59 | MDRLSYAIGDKAVLNNIRVQFQPGSVTALLGPNGAGKSTLLKALCQEIPSAQGSIKLGHCQLVDWPRAELAKSLAVLPQHASLTFPFTVDEVVAMGLYPLTLSQKEGQQLVTKWLAEVGVLHLARRSYPTLSGGEKQRVQLARVLTQLSQSPFPPILLLDEPTSALDLAQQHKVLALAKNLAHKHAYTVIVVLHDLNQAARYSDRVIVLKQGEIVSEGTPNDALSIDIIRQVWDYEPEFIPAPQGDYPLIF | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27509
Sequence Length: 251
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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O60506 | MATEHVNGNGTEEPMDTTSAVIHSENFQTLLDAGLPQKVAEKLDEIYVAGLVAHSDLDERAIEALKEFNEDGALAVLQQFKDSDLSHVQNKSAFLCGVMKTYRQREKQGTKVADSSKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGQQPSVGTEIFVGKIPRDLFEDELVPLFEKAGPIWDLRLMMDPLTGLNRGYAFVTFCTKEAAQEAVKLYNNHEIRSGKHIGVCISVANNRLFVGSIPKSKTKEQILEEFSKVTEGLTDVILYHQPDDKKKNRGFCFLEYEDHKTAAQARRRLMSGKVKVWGNVGTVEWADPIEDPDPEVMAKVKVLFVRNLANTVTEEILEKAFSQFGKLERVKKLKDYAFIHFDERDGAVKAMEEMNGKDLEGENIEIVFAKPPDQKRKERKAQRQAAKNQMYDDYYYYGPPHMPPPTRGRGRGGRGGYGYPPDYYGYEDYYDYYGYDYHNYRGGYEDPYYGYEDFQVGARGRGGRGARGAAPSRGRGAAPPRGRAGYSQRGGPGSARGVRGARGGAQQQRGRGVRGARGGRGGNVGGKRKADGYNQPDSKRRQTNNQNWGSQPIAQQPLQGGDHSGNYGYKSENQEFYQDTFGQQWK | Function: Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences. Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation; seems not to be essential for GAIT complex function.
PTM: Phosphorylated on tyrosine. The membrane-bound form found in microsomes is phosphorylated in vitro by insulin receptor tyrosine kinase (INSR). Phosphorylation is inhibited upon binding to RNA, whereas the cytoplasmic form is poorly phosphorylated (By similarity).
Sequence Mass (Da): 69603
Sequence Length: 623
Domain: The domain containing eight Arg-Gly-Gly repeats (RGG/RXR-box) may be involved in RNA-binding and protein-protein interactions. It is methylated by PRMT1, and essential for nuclear localization.
Subcellular Location: Cytoplasm
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Q7TMK9 | MATEHVNGNGTEEPMDTTSAVIHSENFQTLLDAGLPQKVAEKLDEIYVAGLVAHSDLDERAIEALKEFNEDGALAVLQQFKDSDLSHVQNKSAFLCGVMKTYRQREKQGTKVADSSKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGQQPSVGTEIFVGKIPRDLFEDELVPLFEKAGPIWDLRLMMDPLTGLNRGYAFVTFCTKEAAQEAVKLYNNHEIRSGKHIGVCISVANNRLFVGSIPKSKTKEQILEEFSKVTEGLTDVILYHQPDDKKKNRGFCFLEYEDHKTAAQARRRLMSGKVKVWGNVGTVEWADPIEDPDPEVMAKVKVLFVRNLANTVTEEILEKSFSQFGKLERVKKLKDYAFIHFDERDGAVKAMEEMNGKDLEGENIEIVFAKPPDQKRKERKAQRQAAKNQMYDDYYYYGPPHMPPPTRGRGRGGRGGYGYPPDYYGYEDYYDYYGYDYHNYRGGYEDPYYGYEDFQVGARGRGGRGARGAAPSRGRGAAPPRGRAGYSQRGGPGSARGVRGARGGAQQQRGRGVRGARGGRGGNVGGKRKADGYNQPDTKRRQTNNQNWGSQPIAQQPLQGGDHSGNYGYKSENQEFYQDTFGQQWK | Function: Heterogeneous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1 and isoform 2 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences (By similarity). Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself (By similarity). May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain (By similarity). Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 2 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins.
PTM: Phosphorylated on tyrosine. The membrane-bound form found in microsomes is phosphorylated in vitro by insulin receptor tyrosine kinase (INSR). Phosphorylation is inhibited upon binding to RNA, whereas the cytoplasmic form is poorly phosphorylated.
Sequence Mass (Da): 69633
Sequence Length: 623
Domain: The domain containing eight Arg-Gly-Gly repeats (RGG/RXR-box) may be involved in RNA-binding and protein-protein interactions. It is methylated by PRMT1, and essential for nuclear localization (By similarity).
Subcellular Location: Nucleus
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Q7TP47 | MATEHVNGNGTEEPMDTTSAVIHSENFQTLLDAGLPQKVAEKLDEIYVAGQRKYGGPPPDSVYSGQQPSVGTEIFVGKIPRDLFEDELVPLFEKAGPIWDLRLMMDPLTGLNRGYAFVTFCTKEAAQEAVKLYNNHEIRSGKHIGVCISVANNRLFVGSIPKSKTKEQILEEFSKVTEGLTDVILYHQPDDKKKNRGFCFLEYEDHKTAAQARRRLMSGKVKVWGNVGTVEWADPIEDPDPEVMAKVKVLFVRNLANTVTEEILEKSFSQFGKLERVKKLKDYAFIHFDERDGAVKAMEEMNGKDLEGENIEIVFAKPPDQKRKERKAQRQAAKNQMYDDYYYYGPPHMPPPTRGRGRGGRGGYGYPPDYYGYEDYYDYYGYDYHNYRGGYEDPYYGYEDFQVGARGRGGRGARGAAPSRGRGAAPPRGRAGYSQRGGPGSARGVRGARGGAQQQRGRGVRGARGGRGGNVGGKRKADGYNQPDSKRRQTNNQNWGSQPIAQQPLQGGDHSGNYGYKSENEEFYQDTFGQQWK | Function: Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Is associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Binds to apoB mRNA AU-rich sequences. Part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. May be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins (By similarity).
PTM: Phosphorylated on tyrosine. The membrane-bound form found in microsomes is phosphorylated in vitro by insulin receptor tyrosine kinase (INSR). Phosphorylation is inhibited upon binding to RNA, whereas the cytoplasmic form is poorly phosphorylated.
Sequence Mass (Da): 59710
Sequence Length: 533
Domain: The domain containing eight Arg-Gly-Gly repeats (RGG/RXR-box) may be involved in RNA-binding and protein-protein interactions. It is methylated by PRMT1, and essential for nuclear localization (By similarity).
Subcellular Location: Nucleus
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Q00839 | MSSSPVNVKKLKVSELKEELKKRRLSDKGLKAELMERLQAALDDEEAGGRPAMEPGNGSLDLGGDSAGRSGAGLEQEAAAGGDEEEEEEEEEEEGISALDGDQMELGEENGAAGAADSGPMEEEEAASEDENGDDQGFQEGEDELGDEEEGAGDENGHGEQQPQPPATQQQQPQQQRGAAKEAAGKSSGPTSLFAVTVAPPGARQGQQQAGGKKKAEGGGGGGRPGAPAAGDGKTEQKGGDKKRGVKRPREDHGRGYFEYIEENKYSRAKSPQPPVEEEDEHFDDTVVCLDTYNCDLHFKISRDRLSASSLTMESFAFLWAGGRASYGVSKGKVCFEMKVTEKIPVRHLYTKDIDIHEVRIGWSLTTSGMLLGEEEFSYGYSLKGIKTCNCETEDYGEKFDENDVITCFANFESDEVELSYAKNGQDLGVAFKISKEVLAGRPLFPHVLCHNCAVEFNFGQKEKPYFPIPEEYTFIQNVPLEDRVRGPKGPEEKKDCEVVMMIGLPGAGKTTWVTKHAAENPGKYNILGTNTIMDKMMVAGFKKQMADTGKLNTLLQRAPQCLGKFIEIAARKKRNFILDQTNVSAAAQRRKMCLFAGFQRKAVVVCPKDEDYKQRTQKKAEVEGKDLPEHAVLKMKGNFTLPEVAECFDEITYVELQKEEAQKLLEQYKEESKKALPPEKKQNTGSKKSNKNKSGKNQFNRGGGHRGRGGFNMRGGNFRGGAPGNRGGYNRRGNMPQRGGGGGGSGGIGYPYPRAPVFPGRGSYSNRGNYNRGGMPNRGNYNQNFRGRGNNRGYKNQSQGYNQWQQGQFWGQKPWSQHYHQGYY | Function: DNA- and RNA-binding protein involved in several cellular processes such as nuclear chromatin organization, telomere-length regulation, transcription, mRNA alternative splicing and stability, Xist-mediated transcriptional silencing and mitotic cell progression . Plays a role in the regulation of interphase large-scale gene-rich chromatin organization through chromatin-associated RNAs (caRNAs) in a transcription-dependent manner, and thereby maintains genomic stability . Required for the localization of the long non-coding Xist RNA on the inactive chromosome X (Xi) and the subsequent initiation and maintenance of X-linked transcriptional gene silencing during X-inactivation (By similarity). Plays a role as a RNA polymerase II (Pol II) holoenzyme transcription regulator . Promotes transcription initiation by direct association with the core-TFIIH basal transcription factor complex for the assembly of a functional pre-initiation complex with Pol II in a actin-dependent manner . Blocks Pol II transcription elongation activity by inhibiting the C-terminal domain (CTD) phosphorylation of Pol II and dissociates from Pol II pre-initiation complex prior to productive transcription elongation . Positively regulates CBX5-induced transcriptional gene silencing and retention of CBX5 in the nucleus . Negatively regulates glucocorticoid-mediated transcriptional activation . Key regulator of transcription initiation and elongation in embryonic stem cells upon leukemia inhibitory factor (LIF) signaling (By similarity). Involved in the long non-coding RNA H19-mediated Pol II transcriptional repression . Participates in the circadian regulation of the core clock component BMAL1 transcription (By similarity). Plays a role in the regulation of telomere length . Plays a role as a global pre-mRNA alternative splicing modulator by regulating U2 small nuclear ribonucleoprotein (snRNP) biogenesis . Plays a role in mRNA stability . Component of the CRD-mediated complex that promotes MYC mRNA stabilization . Enhances the expression of specific genes, such as tumor necrosis factor TNFA, by regulating mRNA stability, possibly through binding to the 3'-untranslated region (UTR) . Plays a role in mitotic cell cycle regulation . Involved in the formation of stable mitotic spindle microtubules (MTs) attachment to kinetochore, spindle organization and chromosome congression . Phosphorylation at Ser-59 by PLK1 is required for chromosome alignement and segregation and progression through mitosis . Contributes also to the targeting of AURKA to mitotic spindle MTs . Binds to double- and single-stranded DNA and RNA, poly(A), poly(C) and poly(G) oligoribonucleotides . Binds to chromatin-associated RNAs (caRNAs) . Associates with chromatin to scaffold/matrix attachment region (S/MAR) elements in a chromatin-associated RNAs (caRNAs)-dependent manner . Binds to the Xist RNA . Binds the long non-coding H19 RNA . Binds to SMN1/2 pre-mRNAs at G/U-rich regions . Binds to small nuclear RNAs (snRNAs) . Binds to the 3'-UTR of TNFA mRNA . Binds (via RNA-binding RGG-box region) to the long non-coding Xist RNA; this binding is direct and bridges the Xist RNA and the inactive chromosome X (Xi) (By similarity). Also negatively regulates embryonic stem cell differentiation upon LIF signaling (By similarity). Required for embryonic development (By similarity). Binds to brown fat long non-coding RNA 1 (Blnc1); facilitates the recruitment of Blnc1 by ZBTB7B required to drive brown and beige fat development and thermogenesis (By similarity).
PTM: Cleaved at Asp-100 by CASP3 during T-cell apoptosis, resulting in a loss of DNA- and chromatin-binding activities .
Sequence Mass (Da): 90584
Sequence Length: 825
Domain: The SAP domain is necessary for specific binding to nuclear scaffold/matrix attachment region (S/MAR) elements in DNA . The RNA-binding RGG-box region is necessary for its association with inactive X chromosome (Xi) regions and to chromatin-associated RNAs (caRNAs) . Both the DNA-binding domain SAP and the RNA-binding RGG-box region are necessary for the localization of Xist RNA on the Xi (By similarity). The ATPase and RNA-binding RGG-box regions are necessary for oligomerization .
Subcellular Location: Nucleus
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Q0QLF7 | MFKIDEEKCKKCRMCVKECPVHAVYYEKKDKGAIVEITEKCVECGICKRVCKFGAIENDAPLESVITCSSCPIQCKVPLGETGACTRYRNVGGKLVRDRELVVEALEQKEAADNIKKPIITAVGAGTNYPCSKPAPHIVSECRDGVDVVTVVTEAPLSYSGLVIKLDTNTYIGEEGDPVYRDGKVVGMVNTEEYGSKMIAIGGANRLTGDNGFATARTIVELANGEEVELKVNKKIVLKLKAGVAPVIDGVEESIMRIGCGSATVGLFAKRMKDAVDECIVIDHHVIGLCSEHLAGEAVGMTWSGIIPNATKSSRGRYFGGHGSGIGGTSLETPRDAIKGADMSIAKAGMQVMVVNTTGEIYALFELKADGSFDEIPMTEAALGVALAIQDNCQRSMTSILYTGGTGGSARGGVCTHPVKITEAVHEQKAVLTIGGAPAFVYPGGGINFMVDTQKVVNKAFTWVPTPATVAPVEYTMTVADYEAMGGHMDQIKDVSEYK | Cofactor: Binds 1 flavin covalently per subunit.
Function: Catalyzes the reversible reduction of 6-hydroxynicotinate to 6-oxo-1,4,5,6-tetrahydronicotinate.
Catalytic Activity: 1,4,5,6-tetrahydro-6-oxonicotinate + oxidized 2[4Fe-4S]-[ferredoxin] = 6-hydroxynicotinate + 2 H(+) + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 53097
Sequence Length: 499
Pathway: Cofactor degradation; nicotinate degradation; propanoate and pyruvate from 6-hydroxynicotinate: step 1/8.
EC: 1.3.7.1
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D8LQS7 | MQRVGAASPTCSSLQAPAAAPPILTISPHHRVKTAETAAEPDLLEPTGVHHPFHSLSPLTEARAWAAREGQYFNGLIEANGGASVSKGHPDLAVTFLTDHASCEWFFSQRQEVLDRQDGAYFGPLKCKKQYIGESLPTLASNQKESHQVLREHKLRVFRSRVPFAQSAMTNATDTFYKNLRDNGTGDYTVVYDFFLQQTIHFLHEWIYGLGVEGGQPLPPFKDFMNANPLDVSVLLELEMDTPVANLAAKLAQRSKKPSAEQLASVESIAEAIRSSDVWAGFVEMLEDSNVNTKDLERSFMFTTNFQSAGAIAKGMMPVVATLTNNPEFLEKLRKEVDGKDLTFQSIRGAENFPLLDSFHWEINRMFPAPAFTVKEAKMDLVVPTSSGKKYKVKKGELLMMEQALGQMDPSVFGPDAREFNPERFVDNPELKKKVFAYGYVDHDKVDGQWGCAAHAIGMLDGILKIIYGRWVQEAEWELTSVPVISPDEFLAEVGPADMSFAKVTSRKKM | Function: Cytochrome P450 hydroperoxide bicyclase involved in the metabolism of oxylipins 'ectocarpins' natural products, such as hybridalactone, ecklonilactones and derivatives . Isomerizes the hydroperoxides into epoxyalcohols via epoxyallylic radical . Can use alpha-linolenic acid 13(S)-hydroperoxide (13-HPOTE) and eicosapentaenoic acid 15(S)-hydroperoxide (15-HPEPE) as preferred substrate to produce corresponding heterobicyclic oxylipins, such as plasmodiophorol A (6-oxabicyclo[3.1.0]hexane), plasmodiophorol B (2-oxabicyclo[2.2.1]heptane) and plasmodiophorol C (4-hydroxymethyl-1,2-dihydroxycyclopentane) as well as ectocarpin A (3-propenyl-6-oxabicyclo[3.1.0]hexane) formed at about 15:3:3:1 ratio for 13-HPOTE, and analogous to plasmodiophorols A and B including ectocarpin B (3-[(1'E)-propenyl]-6-oxabicyclo[3.1.0]hexane), ectocarpin C, 14-oxo-15-hydroxy-5,8,11,17-eicosate-traenoic acid and ectocarpin D for 15-HPEPE . Barely able to use linoleic acid 13-hydroperoxide (13-HPODE), linoleic acid 9-hydroperoxide (9-HPODE), eicosapentaenoic acid 15-hydroperoxide (15-HPEPE), and alpha-linolenic acid 9-hydroperoxide (9-HPOTE) as substrates .
Catalytic Activity: (13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate = plasmodiophorol A
Sequence Mass (Da): 56711
Sequence Length: 510
Pathway: Lipid metabolism; oxylipin biosynthesis.
Subcellular Location: Mitochondrion
EC: 4.2.1.-
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Q8GZ99 | MSSRTGASLLLILFFFQICSVSALTNGLDASALNALKSEWTTPPDGWEGSDPCGTNWVGITCQNDRVVSISLGNLDLEGKLPADISFLSELRILDLSYNPKLSGPLPPNIGNLGKLRNLILVGCSFSGQIPESIGTLKELIYLSLNLNKFSGTIPPSIGLLSKLYWFDIADNQIEGELPVSNGTSAPGLDMLLQTKHFHFGKNKLSGNIPKELFSSNMSLIHVLFDGNQFTGEIPETLSLVKTLTVLRLDRNKLIGDIPSYLNNLTNLNELYLANNRFTGTLPNLTSLTSLYTLDVSNNTLDFSPIPSWISSLPSLSTLRMEGIQLNGPIPISFFSPPQLQTVILKRNSIVESLDFGTDVSSQLEFVDLQYNEITDYKPSANKVLQVILANNPVCLEAGNGPSYCSAIQHNTSFSTLPTNCSPCEPGMEASPTCRCAYPFMGTLYFRSPSFSGLFNSTNFSILQKAIADFFKKFNYPVDSVGVRNIRENPTDHQLLIDLLVFPLGRESFNQTGMSLVGFAFSNQTYKPPPIFGPYIFKADLYKQFSDVEVSSKSSNKSILIGAVVGVVVLLLLLTIAGIYALRQKKRAERATGQNNPFAKWDTSKSSIDAPQLMGAKAFTFEELKKCTDNFSEANDVGGGGYGKVYRGILPNGQLIAIKRAQQGSLQGGLEFKTEIELLSRVHHKNVVRLLGFCFDRNEQMLVYEYISNGSLKDSLSGKSGIRLDWTRRLKIALGSGKGLAYLHELADPPIIHRDIKSNNILLDENLTAKVADFGLSKLVGDPEKTHVTTQVKGTMGYLDPEYYMTNQLTEKSDVYGFGVVLLELLTGRSPIERGKYVVREVKTKMNKSRSLYDLQELLDTTIIASSGNLKGFEKYVDLALRCVEEEGVNRPSMGEVVKEIENIMQLAGLNPNSDSATSSRTYEDAIKGSGDPYGSESFQYSGNFPASKLEPQ | Function: Leucine-rich repeat receptor protein kinase that acts as sensor of extracellular hydrogen peroxide . Required for intracellular calcium influx in response to extracellular hydrogen peroxide . Mediates hydrogen peroxide-induced activation of calcium channels in guard cells and is required for stomatal closure .
PTM: Autophosphorylated at Ser-606, Ser-607, Thr-786, Thr-789, Thr-790 and Ser-942 in response to extracellular hydrogen peroxide.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 104708
Sequence Length: 953
Subcellular Location: Cell membrane
EC: 2.7.11.1
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A9A2G6 | MAAVKKIFDEIIETDHKVITEESSKSILKNYGVKVPPYALVTSAEEAAKEAKKIGFPLVMKVVSPQILHKTDVGGVKVGLDNVADVKKTFTDMYGRLSKKKGVNVKGILLEKMVPKGVELIVGIQNDSQFGPIIMVGMGGIMTEVMKDVAFRMLPITTSDAKSMLNELKGSKLLKGFRGSEPIDTNLVAKMLVNIGKLGVENADYINSIDFNPVIVYPKSHYVVDAKIILNKEKKKNSISKAKPSITDMETFFTPKSVALVGASASPGKIGNSILDSLVNYDFKGKVYPINPKADKIFGQKCYPSVADIPGKVDLVVVSVDLSMTPPVLEDCAKKGVHSVVIVSGGGKELGGERAAYEAEVARLSKKHKIRIIGPNCIGMFNAANRLDCAFQGQERMVRSKLGPVAFFSQSGTMGISMLESADTFGLSKMISFGNRSDVDEADMIWYAANDPQTKVIGLYVEGFGDGRKFINVAKRVMKEKKKPIVIWKSGRTAAGAKQAASHTGSLGGSNAIIMGAFKQAGIISVDSYQELAGVLKALAWQPAAKGNKVAMTSNGAGPMIGGIDQLEKFGLAIGKLSPKLLKKMKSRFPPAVPIHNGNPADVGGGATADDYQFVIQQFMDEKNIDIAMPWFVFQDDPLEETIVDHLAGFQKKAKKPLLCGGNGGPYTEKMIKLIEKHNVPVYQDLRTWVAAASALHQWGKISKK | Cofactor: No activity with Ni(2+), Co(2+) and Ca(2+).
Function: Involved in thaumarchaeal hydroxypropionate/hydroxybutyrate (HP/HB) cycle, a modified version of the autotrophic HP/HB cycle of Crenarchaeota. Catalyzes the formation of 3-hydroxypropionyl-CoA, ADP and phosphate from 3-hydroxypropionate, coenzyme A (CoA) and ATP. Can also use 4-hydroxybutyrate, propionate and butyrate, with poor catalytic efficiency.
Catalytic Activity: 3-hydroxypropanoate + ATP + CoA = 3-hydroxypropanoyl-CoA + ADP + phosphate
Sequence Mass (Da): 76129
Sequence Length: 705
EC: 6.2.1.-
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A4YGR1 | MFMRYIMVEEQTLKTGSQELEEKADYNMRYYAHLMKLSKEKPAEFWGSLAQDLLDWYEPWKETMRQEDPMTRWFIGGKINASYNAVDRHLNGPRKFKAAVIWESELGERKIVTYQDMFYEVNRWANALRSLGVGKGDRVTIYMPLTPEGIAAMLASARIGAIHSVIFAGFGSQAIADRVEDAKAKVVITADAYPRRGKVVELKKTVDEALNSLGERSPVQHVLVYRRMKTDVNMKEGRDVFFDEVGKYRYVEPERMDSNDPLFILYTSGTTGKPKGIMHSTGGYLTGTAVMLLWSYGLSQENDVLFNTSDIGWIVGHSYITYSPLIMGRTVVIYESAPDYPYPDKWAEIIERYRATTFGTSATALRYFMKYGDEYVKNHDLSSIRIIVTNGEVLNYSPWKWGLEVLGGGKVFMSHQWWQTETGAPNLGYLPGIIYMPMKSGPASGFPLPGNFVEVLDENGNPSAPRVRGYLVMRPPFPPNMMMGMWNDNGERLKKTYFSKFGSLYYPGDFAMVDEDGYIWVLGRADETLKIAAHRIGAGEVESAITSHPSVAEAAVIGVPDSVKGEEVHAFVVLKQGYAPSSELAKDIQSHVRKVMGPIVSPQIHFVDKLPKTRSGKVMRRVIKAVMMGSSAGDLTTIEDEASMDEIKKAVEELKKELKTS | Function: Plays a role in the autotrophic CO(2) fixation pathway. Activates 3-hydroxypropionate to its CoA ester. Can also activate propionate, and to a lesser extent acrylate, acetate and butyrate.
Catalytic Activity: 3-hydroxypropanoate + ATP + CoA = 3-hydroxypropanoyl-CoA + AMP + diphosphate
Sequence Mass (Da): 74402
Sequence Length: 661
EC: 6.2.1.36
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P84074 | MGKQNSKLRPEMLQDLRENTEFSELELQEWYKGFLKDCPTGILNVDEFKKIYANFFPYGDASKFAEHVFRTFDTNSDGTIDFREFIIALSVTSRGRLEQKLMWAFSMYDLDGNGYISREEMLEIVQAIYKMVSSVMKMPEDESTPEKRTEKIFRQMDTNNDGKLSLEEFIRGAKSDPSIVRLLQCDPSSASQF | Function: Calcium-binding protein that may play a role in the regulation of voltage-dependent calcium channels . May also play a role in cyclic-nucleotide-mediated signaling through the regulation of adenylate and guanylate cyclases (By similarity).
PTM: Myristoylation facilitates association with membranes.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22427
Sequence Length: 193
Domain: Binds 3 calcium via EF-hand domains. The cryptic EF-hand 1 does not bind calcium.
Subcellular Location: Cytoplasm
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Q05353 | MGKLALAAKITHVPSMYLSELPGKNHGCRQGAIDGHKEISKRCREMGVDTIIVFDTHWLVNSAYHINCADHFEGVYTSNELPHFIRDMTYNYEGNPELGQLIADEALKLGVRAKAHNIPSLKLEYGSVVPMRYMNEDKRFKVVSISAFCTVHDFADSRKLGERIVKAIEQYDGTVAVLASGSLSHRFIDDQRAEEGMNSYTREFDRQMDERVVKLWREGQFKEFCNMLPEYADYCYGEGNMHDTVMLLGMLGWDKYDGKVWSLSPSYSQASWHRSG | Function: Transforms homoprotocatechuic acid (HPC) into 5-carboxymethyl-2-hydroxy-muconic semialdehyde (CHMS).
Catalytic Activity: 3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde + H(+)
Sequence Mass (Da): 31495
Sequence Length: 276
Pathway: Aromatic compound metabolism; 4-hydroxyphenylacetate degradation; pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate: step 2/7.
EC: 1.13.11.15
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P42269 | MKKVNHWINGKNVAGNDYFLTTNPATGEVLADVASGGEAEINQAVATAKEAFPKWANLPMKERARLMRRLGDLIDQNVPEIAAMETADTGLPIHQTKNVLIPRASHNFEFFAEVCQQMNGKTYPVDDKMLNYTLVQPVGVCALVSPWNVPFMTATWKVAPCLALGITAVLKMSELSPLTADRLGELALEAGIPAGVLNVVQGYGATAGDALVRHHDVRAVSFTGGTATGRNIMKNAGLKKYSMELGGKSPVLIFEDADIERALDAALFTIFSINGERCTAGSRIFIQQSIYPEFVKFAERANRVRVGDPTDPNTQVGALISQQHWEKVSGYIRLGIEEGATLLAGGPDKPSDLPAHLKGGNFLRPTVLADVDNRMRVAQEEIFGPVACLLPFKDEAEALRLANDVEYGLASYIWTQDVSKVLRLARGIEAGMVFVNTQFVRDLRHAFGGVKPRTGREGGGYSSKCSRK | Function: Transforms 5-carboxymethyl-2-hydroxy-muconic semialdehyde (CHMS) into 5-carboxymethyl-2-hydroxy-muconic acid (CHM).
Sequence Mass (Da): 50827
Sequence Length: 468
Pathway: Aromatic compound metabolism; 4-hydroxyphenylacetate degradation; pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate: step 3/7.
EC: 1.2.1.-
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Q05354 | MPHFIVECSDNIREEADLPGLFAKVNPTLAATGIFPLAGIRSRVHWVDTWQMADGQHDYASVHMTLKIGAGRSLESRQQAGEMLFELIKTHFAALMESRLLALSFEIEELHPTLNFKQNNVHALFK | Function: Transforms 5-carboxymethyl-2-hydroxy-muconic acid (CHM) into 5-oxo-pent-3-ene-1,2,5-tricarboxylic acid (OPET).
Catalytic Activity: (2E,4Z)-5-hydroxypenta-2,4-diene-1,2,5-tricarboxylate = (3E,5R)-5-carboxy-2-oxohept-3-enedioate
Sequence Mass (Da): 14215
Sequence Length: 126
Pathway: Aromatic compound metabolism; 4-hydroxyphenylacetate degradation; pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate: step 4/7.
EC: 5.3.3.10
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A4YI89 | MEFETIETKKEGNLFWITLNRPDKLNALNAKLLEELDRAVSQAESDPEIRVIIITGKGKAFCAGADITQFNQLTPAEAWKFSKKGREIMDKIEALSKPTIAMINGYALGGGLELALACDIRIAAEEAQLGLPEINLGIYPGYGGTQRLTRVIGKGRALEMMMTGDRIPGKDAEKYGLVNRVVPLANLEQETRKLAEKIAKKSPISLALIKEVVNRGLDSPLLSGLALESVGWGVVFSTEDKKEGVSAFLEKREPTFKGK | Function: Plays a role in autotrophic carbon fixation via the 3-hydroxypropionate/4-hydroxybutyrate cycle. Catalyzes the reversible dehydration of 3-hydroxypropionyl-CoA to form acryloyl-CoA, and the reversible dehydration of (S)-3-hydroxybutyryl-CoA to form crotonyl-CoA. Inactive towards (R)-3-hydroxybutyryl-CoA.
Catalytic Activity: 3-hydroxypropanoyl-CoA = acryloyl-CoA + H2O
Sequence Mass (Da): 28316
Sequence Length: 259
EC: 4.2.1.116
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P32755 | MTTYSNKGPKPERGRFLHFHSVTFWVGNAKQAASFYCNKMGFEPLAYKGLETGSREVVSHVIKQGKIVFVLCSALNPWNKEMGDHLVKHGDGVKDIAFEVEDCEHIVQKARERGAKIVREPWVEEDKFGKVKFAVLQTYGDTTHTLVEKINYTGRFLPGFEAPTYKDTLLPKLPSCNLEIIDHIVGNQPDQEMESASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVANYEESIKMPINEPAPGRKKSQIQEYVDYNGGAGVQHIALRTEDIITTIRHLRERGMEFLAVPSSYYRLLRENLKTSKIQVKENMDVLEELKILVDYDEKGYLLQIFTKPMQDRPTLFLEVIQRHNHQGFGAGNFNSLFKAFEEEQALRGNLTDLETNGVRSGM | Cofactor: Binds 1 Fe cation per subunit.
Function: Catalyzes the conversion of 4-hydroxyphenylpyruvic acid to homogentisic acid, one of the steps in tyrosine catabolism.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45112
Sequence Length: 393
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
Subcellular Location: Cytoplasm
EC: 1.13.11.27
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Q53586 | MTQTTHHTPDTARQADPFPVKGMDAVVFAVGNAKQAAHYYSTAFGMQLVAYSGPENGSRETASYVLTNGSARFVLTSVIKPATPWGHFLADHVAEHGDGVVDLAIEVPDARAAHAYAIEHGARSVAEPYELKDEHGTVVLAAIATYGKTRHTLVDRTGYDGPYLPGYVAAAPIVEPPAHRTFQAIDHCVGNVELGRMNEWVGFYNKVMGFTNMKEFVGDDIATEYSALMSKVVADGTLKVKFPINEPALAKKKSQIDEYLEFYGGAGVQHIALNTGDIVETVRTMRAAGVQFLDTPDSYYDTLGEWVGDTRVPVDTLRELKILADRDEDGYLLQIFTKPVQDRPTVFFEIIERHGSMGFGKGNFKALFEAIEREQEKRGNL | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 41863
Sequence Length: 381
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
EC: 1.13.11.27
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Q27203 | MSENKDHVVVGYTEKPVGERPTGGKFLGYDHLHFWVGNAKQAAGWYTSRFGFEYYAYKGLETGSREVATHVVRNKQGVTLAFSTPYGNDKDNQREMNQHQSLHGDGVKDVAFAVEDCHSIYNKAIQRGAKCAYPPQDLKDEHGSVTIAAVHTYGEVIHTFIQRNDYKGFFMPGFVAHPLKDPLNNVLPDISYNYVDHIVGNQPDNMMTSAADWYEKTLDFHRFWSVDDSMIHTEFSSLRSIVMTDYDQKIKMPINEPADGKRKSQIQEYIDFYAGPGVQHIALNTSDVINTVEGLRARGVEFLSIPTSYYDNLRKALTAQTSITVKEDLDVLQKNHILVDYDEKGYLLQIFTKPVEDRPTLFYEIIQRNNHQGFGAGNFKSLFVSLELEQEKRGNLTEIVKNIY | Cofactor: Binds 1 Fe cation per subunit.
Function: Key enzyme in the degradation of tyrosine.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 46046
Sequence Length: 404
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
EC: 1.13.11.27
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O42764 | MAPGALLVTSQNGRTSPLYDSDGYVPAPAALVVGGEVNYRGYHHAEWWVGNAKQVAQFYITRMGFEPVAHKGLETGSRFFASHVVQNNGVRFVFTSPVRSSARQTLKAAPLADQARLDEMYDHLDKHGDGVKDVAFEVDDVLAVYENAVANGAESVSSPHTDSCDEGDVISAAIKTYGDTTHTFIQRTTYTGPFLPGYRSCTTVDSANKFLPPVNLEAIDHCVGNQDWDEMSDACDFYERCLGFHRFWSVDDKDICTEFSALKSIVMSSPNQVVKMPINEPAHGKKKSQIEEYVDFYNGPGVQHIALRTPNIIEAVSNLRSRGVEFISVPDTYYENMRLRLKAAGMKLEESFDIIQKLNILIDFDEGGYLLQLFTKPLMDRPTVFIEIIQRNNFDGFGAGNFKSLFEAIEREQDLRGNL | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 46740
Sequence Length: 419
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
EC: 1.13.11.27
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Q9JN69 | MDVRTLAVGKAHLEALLATRKMTLEHLQDVRHDATQVYFDGLEHLQNVAQYLAIPLSEFFVGQTQSDLDDGVKIARRNGGFKREEIRGGVHYYTYEHLVTTNQDPGLMALRLDLHSDDEQPLRLNGGHGSREIVYVTRGAVRVRWVGDNDELKEDVLNEGDSIFILPNVPHSFTNHVGGAKSEIIAINYG | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Non-heme-dependent dioxygenase that catalyzes the oxidative epoxidation of (S)-2-hydroxypropylphosphonate into (1R,2S)-epoxypropylphosphonate, the final step in the biosynthesis of fosfomycin antibiotic.
Catalytic Activity: (S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-epoxypropylphosphonate + 2 H2O
Sequence Mass (Da): 21317
Sequence Length: 190
Pathway: Antibiotic biosynthesis; fosfomycin biosynthesis.
EC: 1.11.1.23
|
Q56185 | MSNTKTASTGFAELLKDRREQVKMDHAALASLLGETPETVAAWENGEGGELTLTQLGRIAHVLGTSIGALTPPAGNDLDDGVIIQMPDERPILKGVRDNVDYYVYNCLVRTKRAPSLVPLVVDVLTDNPDDAKFNSGHAGNEFLFVLEGEIHMKWGDKENPKEALLPTGASMFVEEHVPHAFTAAKGTGSAKLIAVNF | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Non-heme-dependent dioxygenase that catalyzes the oxidative epoxidation of (S)-2-hydroxypropylphosphonate into (1R,2S)-epoxypropylphosphonate, the final step in the biosynthesis of fosfomycin antibiotic.
Catalytic Activity: (S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-epoxypropylphosphonate + 2 H2O
Sequence Mass (Da): 21337
Sequence Length: 198
Pathway: Antibiotic biosynthesis; fosfomycin biosynthesis.
EC: 1.11.1.23
|
O66550 | MATVYLGLGSNVGDRISYILKAIEKLEEFLEIEKISTVYESKAWGFENQGNFLNFVLKAKTSLLPQELLLKIKKVEKEVGRKERFKWGPREIDIDILLYKDEVIRTKLLKVPHPFLEKRDFFVYPLLEIEPNVIHPIYRKPLKEFKPENTLKPFCCILKV | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 18838
Sequence Length: 160
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
EC: 2.7.6.3
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P29252 | MNNIAYIALGSNIGDRETYLRQAVALLHQHAAVTVTKVSSIYETDPVGYEDQAQFLNMAVEIKTSLNPFELLELTQQIENELGRTREVRWGPRTADLDILLFNRENIETEQLIVPHPRMYERLFVLAPLAEICQQVEKEATSAETDQEGVRVWKQKSGVDEFVHSES | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 19058
Sequence Length: 167
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
EC: 2.7.6.3
|
Q9PJ54 | MLKIQGVKHFEKSRFFPFFSQNIRSFKYLALIGLGSNIEPEKKRFDMLFRVMMDDKRFKILSTSPMLINEAFGFKEQKDFTNAVMLIQTNLHARALLKVLLYYEVKFKRKRTFKNAPRTLDLDLLYFSQKVKRDKWCEVPHKGAKERVSVILPLGMI | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 18628
Sequence Length: 157
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
EC: 2.7.6.3
|
P26281 | MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIMLFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 18079
Sequence Length: 159
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
EC: 2.7.6.3
|
P43777 | MITAYIALGSNLNTPVEQLHAALKAISQLSNTHLVTTSSFYKSKPLGPQDQPDYVNAVAKIETELSPLKLLDELQRIENEQGRVRLRRWGERTLDLDILLYGNEIIQNERLTIPHYDMHNREFVIVPLFEIASDLVLPNSQIITELVKQFADHKMIKLNP | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 18299
Sequence Length: 160
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
EC: 2.7.6.3
|
O25680 | MMREILTSRFFPSLFKKRLDFSNRVVLGLGSNLKNPLKILKNCFLYFKNHSKIGKIFSSPIYINPPFGYTKQPNFYNATIILKTSLSLRHFFALVFYIERRFGRQRKRDFKDAPRTLDIDIIAFNQVILRQNDLALPHPKWSERDSVLVPLALQQILFKKGEW | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 19282
Sequence Length: 163
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
EC: 2.7.6.3
|
P71512 | MTRAYLGLGSNIGDKAAMLAGAVEHLAATPGIRVVARSADYRTPPWGDTDQDWFLNAAVAIDTELTPHGLLEVCLSIEAALGRVRERRWGPRVIDIDVLAYEGAQVSDERLVLPHRFVRERAFVLVPLAEIAPDLVIGGETVREALAKLDPSGIERVE | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 17206
Sequence Length: 158
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
EC: 2.7.6.3
|
O69528 | MTRVVLSIGSNLGDRLAWLQSAVDGLGDAVVAVSPVYDTVPWGAVEQRSFLNAVVIADGPAYDTKAWLCRAQELERNAGRVRGQRWGARTLDVDLISCYQTSGATTGAVEVITCESNLTLPHPRAHLRAFVLVPWLAVDSDAELTVAGRAQRVDRLLAEMEPTEREGVRLTNLTLKLKRSSPARPVSPKSD | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 20761
Sequence Length: 191
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
EC: 2.7.6.3
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P61325 | MEKFTIKDLTDNLKFEIISGQDKLDTEIKSYGINRAGLELADYFKPFKDQSEWRATLMSTKESGYMLQFDEETKIKKYTQLMKCGIPVLIITNKFKDKTLIKVAKRLNFPLLRSDYPITIQLVQKIQDIYDIYFSPTAEEHAALMNIFGTGVLIKGKSGIGKSELCLDLIKHNHLFIGDDRIILTNKSNKIIGRVHPILKNLIEIRGIGIFDIVKSNGYQVIMNESPVELVVELVEYKEQNIDNSDRLGNDWSKFKILGVEIEHIQIPVSAGRSLVNIIESAVAQFKINKSKQFENVFDVIHKRTKEFLSSKK | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Therefore, by controlling the phosphorylation state of HPr, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion.
Catalytic Activity: [HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-serine + ADP + H(+)
Sequence Mass (Da): 35876
Sequence Length: 313
Domain: The Walker A ATP-binding motif also binds Pi and PPi.
EC: 2.7.11.-
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P75548 | MKKLLVKELIEQFQDCVNLIDGHTNTSNVIRVPGLKRVVFEMLGLFSSQIGSVAILGKREFGFLSQKTLVEQQQILHNLLKLNPPAIILTKSFTDPTVLLQVNQTYQVPILKTDFFSTELSFTVETYINEQFATVAQIHGVLLEVFGVGVLLTGRSGIGKSECALDLINKNHLFVGDDAIEIYRLGNRLFGRAQEVAKKFMEIRGLGIINVERFYGLQITKQRTEIQLMVNLLSLEKQTTVTFERLGTELKKQRLLGVDLSFYEIPISPGRKTSEIIESAVIDFKLKHSGYNSALDFIENQKAILKRKKDES | Function: Is a metabolite-sensitive enzyme that catalyzes the ATP-as well as probably the pyrophosphate-dependent phosphorylation of Ser-47 in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The regulatory role of HPrK/P in the physiology of M.pneumoniae is not known yet.
Catalytic Activity: [HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-serine + ADP + H(+)
Sequence Mass (Da): 35234
Sequence Length: 312
Domain: The Walker A ATP-binding motif also binds Pi and PPi.
EC: 2.7.11.-
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Q98PL1 | MKKKLFVSELIKHFDLEVLNHDFPEIEDREILTPSIKRLGLELSGHFIYDAISGVIVGWGTNESKFFEKIGSEKAKSSIEEIFSRKIPMLVLSKGFDKNYYSTIIEIANKHKTPVIFYKASLSEINTILGIYLLQYFAKKVQVHGTLVSVFGMGILIVGDSGLGKSEAALELVQKGHVLISDDAVLVSHYGNKYFGKAPYITKNLIEVRGLGLIDILSVHGLKSVLPECEINFVVELKDYEQNKSNFDRLGNKVLKYQIGEWKIPKIEIPIRQGRSVASLIEASANMFLSKLNGHDVLAMIQERSLNDE | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr) (By similarity).
Catalytic Activity: [HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-serine + ADP + H(+)
Sequence Mass (Da): 34716
Sequence Length: 309
Domain: The Walker A ATP-binding motif also binds Pi and PPi.
EC: 2.7.11.-
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Q9K081 | MPSISVRRLFDDNQYKLQLAWAAGNSGADNRIGVEADKPVLALVGHLNFIHPNQIQVVGLAESEYLNRLESGETGYQFGDLFDISMSLVIVANGLPVSPGLRDYCHKNDIPLLTSKLESPYLMDVLRIYLQRTLAASSVKHGVFLDVFEIGVLITGHSGLGKSELALELISRGHSLIADDAVELFRIGPETLEGRCSPMLRDFLEVRGLGILNIRHIFGETSIRPKKILQLIINLVEADDEYMKQLDRLSIRTETESILNVNVRSVTLPVAVGRNLAVLVEAAVRNYILQLRGKDSTREFLERHQTQLKENEQHNEDRPD | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr).
Catalytic Activity: [HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-serine + ADP + H(+)
Sequence Mass (Da): 35800
Sequence Length: 320
Domain: The Walker A ATP-binding motif also binds Pi and PPi.
EC: 2.7.11.-
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Q82Y30 | MSQVSITQLFEENQEKLNLQWGEPSAVIDRQLENHQINNSTQELIGHLNFVHPNWIQVLNQTSVNYLDQLDDVSLKKRLNQLAKSQLACLIVADDAPIPNAIRQFVNEQSVPLIQSATASLEIIWRLQSYLARMLAPAITRHGVLLDVLGMGVMITGESGVGKSELALELISRGHGLVADDVVELHRIGPETLEGQCPPLLRDFLEVRGLGMLNIRTIFGETAVRRRKNMKLIVHLEKTVGSSINAYERLPLSNLNEIILNVGIRKVIIPVAAGRNLAVLVEAAVRNYILQLRGIDSTQEFIRRHESEMAGNTAEHFDDSHNE | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr).
Catalytic Activity: [HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-serine + ADP + H(+)
Sequence Mass (Da): 36084
Sequence Length: 323
Domain: The Walker A ATP-binding motif also binds Pi and PPi.
EC: 2.7.11.-
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Q8Y2D1 | MELTGVTAQSIFDDNAADLKLSWVAGLEGADRAFDVDFAKEATSAADLVGHLNLIHPNRIQVLGKPEITYYQRLSEENRKRQMGELILLEPPFLVVADGVDPPPDLELRCTRSSTPLFTSPISSAAVIDHLRLYLSRISAPRVTMHGVFLDILGMGVLIMGDSGLGKSELGLELISRGHGLVADDAVDFVRLGPDFIEGRCPPLLQNLLEVRGLGLLDIKTIFGETAVRRKMKIKLIVQLVRRNDGEFERLPLDSQYMDVLGLPIHMVKIQVAAGRNLAVLVEAAVRNTILRLRGIDTLRDFMDRQRAAMQAEAASHSPQGRLL | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr).
Catalytic Activity: [HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-serine + ADP + H(+)
Sequence Mass (Da): 35684
Sequence Length: 324
Domain: The Walker A ATP-binding motif also binds Pi and PPi.
EC: 2.7.11.-
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O85093 | MSALRLRKVDALLAQATRELGAGQSLGFSAAGQDAELTLLPLLADAGEPAGAVWLSTAIGPLLLSDAEALLSLLGDIPLTLGGEQQAWYWQLFNQRLSPTVARLLAPVEPLHNKPQAPTLGCRVQIRRGGEQLHAHMHATPDTLLRLLRSASWQARTRTVDESWSVASPLIIGEMSLTREQIASLRPGDVVLPAHCQFDSAGQGFLSLAGRQWAAQTDQHAQRLFLRLSHEEHRHHEY | Function: Component of the type III secretion system, which is required for effector protein delivery, parasitism, and pathogenicity. Probably participates in the formation of a C-ring-like assembly along with hrcQb.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25998
Sequence Length: 238
Domain: The HrcQa-C domain interacts with the hrcQb C-terminal domain.
Subcellular Location: Cell inner membrane
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Q4L8L8 | MNLAWKEIKFYRFRYTLIMLIIFLLGSMVLFISGLAQGLARENISYLNNMPAEHYIVEDNKEPKLESSQLNQSQQNKIEKIIHENATQMGTQTLKINQQDQDVITLNTPKHLTPKLVSGNYPKKQNEIAISEKLTGNDLKVGDTVTFKGHHHNYKISGIMNESMYSHSSMILMNKEAFKSLNKQVSTFYPVDKINKDNKESLKQIKGIKVVNEKALTDNIASYQAEQMPLNLMIISLFVITAIVLSAFFYVMTIQKIPQIGILKAIGIKTKHLLTALLLQIILTTMVGVILAFSVILILNAFMPVTMPFYLSYSQVLLMIVVFLIVGLIGALLSFIKVLKVDPIEAIGGME | Function: Part of the ABC transporter complex hrt involved in hemin import. Responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39569
Sequence Length: 351
Subcellular Location: Cell membrane
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Q49ZT7 | MKLAWQEIKYYKFRYILIMLIILLLGIMVLFISGLAQGLARENISMLDNMKSEKYVLQDNKQPQIEKSIIKPEQQNKIEDITGQEPLKMAPQTLKIDKNEEDVLMINTVKNEKPELKAGHYPTKDNEVAINNKLTADGINVGDKIKLKDGKALKVSGVLNDTMYSHSSVVMMSDNGFNTLNKQASTIYPVKDLSKSEQEKVNDISGVKVFTENDITSEIPSYQAEQAPLNMMIVSLFVISAIVLSAFFYVMTIQKIPEIGILKAIGMKTKHLLSALIIQILITTMIGVIISVAIITGLSFLMPVSMPFHVTTSNLLLVVGVFIIVAIIGAILSFIKLFKVDPIEAIGGGE | Function: Part of the ABC transporter complex hrt involved in hemin import. Responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38790
Sequence Length: 350
Subcellular Location: Cell membrane
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O94641 | MADYPFTDKAAKTLSDAYSIAQSYGHSQLTPIHIAAALLSDSDSNGTTLLRTIVDKAGGDGQKFERSVTSRLVRLPAQDPPPEQVTLSPESAKLLRNAHELQKTQKDSYIAQDHFIAVFTKDDTLKSLLAEAGVTPKAFEFAVNNVRGNKRIDSKNAEEGFDALNKFTVDLTELARNGQLDPVIGREDEIRRTIRVLSRRTKNNPVLIGEPGVGKTSIAEGLARRIIDDDVPANLSNCKLLSLDVGSLVAGSKFRGEFEERIKSVLKEVEESETPIILFVDEMHLLMGAGSGGEGGMDAANLLKPMLARGKLHCIGATTLAEYKKYIEKDAAFERRFQIILVKEPSIEDTISILRGLKEKYEVHHGVTISDRALVTAAHLASRYLTSRRLPDSAIDLVDEAAAAVRVTRESQPEVLDNLERKLRQLRVEIRALEREKDEASKERLKAARKEAEQVEEETRPIREKYELEKSRGSELQDAKRRLDELKAKAEDAERRNDFTLAADLKYYGIPDLQKRIEYLEQQKRKADAEAIANAQPGSEPLLIDVVGPDQINEIVARWTGIPVTRLKTTEKERLLNMEKVLSKQVIGQNEAVTAVANAIRLSRAGLSDPNQPIASFLFCGPSGTGKTLLTKALASFMFDDENAMIRIDMSEYMEKHSVSRLIGAPPGYVGHEAGGQLTEQLRRRPYSVILFDEIEKAAPEVLTVLLQVLDDGRITSGQGQVVDAKNAVIIMTSNLGAEYLTTDNESDDGKIDSTTREMVMNSIRGFFRPEFLNRISSIVIFNRLRRVDIRNIVENRILEVQKRLQSNHRSIKIEVSDEAKDLLGSAGYSPAYGARPLNRVIQNQVLNPMAVLILNGQLRDKETAHVVVQNGKIFVKPNHEANANGSADIDMDGIDDDVNDEELE | Function: Required, in concert with Hsp40 and Hsp70 and small Hsps, for the dissociation, resolubilization and refolding of aggregates of damaged proteins after heat or other environmental stresses. Extracts proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by components of the Hsp70/Hsp40 chaperone system (By similarity).
Sequence Mass (Da): 100507
Sequence Length: 905
Domain: Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per monomer. ATP binding to NBD1 triggers binding of polypeptides and stimulates ATP hydrolysis at NBD2. Nucleotide binding to NBD2 is crucial for oligomerization (By similarity).
Subcellular Location: Cytoplasm
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P31539 | MNDQTQFTERALTILTLAQKLASDHQHPQLQPIHILAAFIETPEDGSVPYLQNLIEKGRYDYDLFKKVVNRNLVRIPQQQPAPAEITPSYALGKVLQDAAKIQKQQKDSFIAQDHILFALFNDSSIQQIFKEAQVDIEAIKQQALELRGNTRIDSRGADTNTPLEYLSKYAIDMTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEPGIGKTAIIEGVAQRIIDDDVPTILQGAKLFSLDLAALTAGAKYKGDFEERFKGVLKEIEESKTLIVLFIDEIHMLMGNGKDDAANILKPALSRGQLKVIGATTNNEYRSIVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVRILDSALVTAAQLAKRYLPYRRLPDSALDLVDISCAGVAVARDSKPEELDSKERQLQLIQVEIKALERDEDADSTTKDRLKLARQKEASLQEELEPLRQRYNEEKHGHEELTQAKKKLDELENKALDAERRYDTATAADLRYFAIPDIKKQIEKLEDQVAEEERRAGANSMIQNVVDSDTISETAARLTGIPVKKLSESENEKLIHMERDLSSEVVGQMDAIKAVSNAVRLSRSGLANPRQPASFLFLGLSGSGKTELAKKVAGFLFNDEDMMIRVDCSELSEKYAVSKLLGTTAGYVGYDEGGFLTNQLQYKPYSVLLFDEVEKAHPDVLTVMLQMLDDGRITSGQGKTIDCSNCIVIMTSNLGAEFINSQQGSKIQESTKNLVMGAVRQHFRPEFLNRISSIVIFNKLSRKAIHKIVDIRLKEIEERFEQNDKHYKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLALRILKNEIKDKETVNVVLKKGKSRDENVPEEAEECLEVLPNHEATIGADTLGDDDNEDSMEIDDDLD | Function: Required, in concert with Hsp40 (YDJ1) and Hsp70 (SSA1) and small Hsps (HSP26), for the dissociation, resolubilization and refolding of aggregates of damaged proteins after heat or other environmental stresses. Extracts proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by components of the Hsp70/Hsp40 chaperone system. Substrate binding is ATP-dependent, and release of bound polypeptide is triggered by ATP hydrolysis. Also responsible for the maintenance of prions by dissociating prion fibrils into smaller oligomers, thereby producing transmissible seeds that can infect daughter cells during mitosis and meiosis. Loss of HSP104 can cure yeast cells of the prions [PSI+], [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of [PSI+].
Sequence Mass (Da): 102035
Sequence Length: 908
Domain: Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per monomer, a low-affinity, high-turnover site (NBD1) and a high-affinity site (NBD2) with a 300-fold slower rate of hydrolysis. There is allosteric regulation between the 2 sites. ATP binding to NBD1 triggers binding of polypeptides and stimulates ATP hydrolysis at NBD2. Nucleotide binding to NBD2 is crucial for oligomerization.
Subcellular Location: Cytoplasm
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Q92598 | MSVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQKEKENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILSPAFKVREFSVTDAVPFPISLIWNHDSEDTEGVHEVFSRNHAAPFSKVLTFLRRGPFELEAFYSDPQGVPYPEAKIGRFVVQNVSAQKDGEKSRVKVKVRVNTHGIFTISTASMVEKVPTEENEMSSEADMECLNQRPPENPDTDKNVQQDNSEAGTQPQVQTDAQQTSQSPPSPELTSEENKIPDADKANEKKVDQPPEAKKPKIKVVNVELPIEANLVWQLGKDLLNMYIETEGKMIMQDKLEKERNDAKNAVEEYVYEFRDKLCGPYEKFICEQDHQNFLRLLTETEDWLYEEGEDQAKQAYVDKLEELMKIGTPVKVRFQEAEERPKMFEELGQRLQHYAKIAADFRNKDEKYNHIDESEMKKVEKSVNEVMEWMNNVMNAQAKKSLDQDPVVRAQEIKTKIKELNNTCEPVVTQPKPKIESPKLERTPNGPNIDKKEEDLEDKNNFGAEPPHQNGECYPNEKNSVNMDLD | Function: Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release . Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity).
PTM: Phosphorylation on Ser-509 may be important for regulation of the HSPA8/HSC70 chaperone activity.
Sequence Mass (Da): 96865
Sequence Length: 858
Subcellular Location: Cytoplasm
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Q61699 | MSVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSSFKRFHGRAFNDPFIQKEKENLSYDLVPMKNGGVGIKVMYMDEEHFFSVEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMTAVALNYGIYKQDLPNAEEKPRVVVFVDMGHSSFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVEHFCAEFKTKYKLDAKSKIRALLRLHQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPLHSLMAQTQLKAEDVSAIEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQCAILSPAFKVREFSVTDAVPFPISLVWNHDSEETEGVHEVFSRNHAAPFSKVLTFLRRGPFELEAFYSDPQGVPYPEAKIGRFVVQNVSAQKDGEKSRVKVKVRVNTHGIFTISTASMVEKVPTEEEDGSSLEADMECPNQRPTESSDVDKNIQQDNSEAGTQPQVQTDGQQTSQSPPSPELTSEESKTPDADKANEKKVDQPPEAKKPKIKVVNVELPVEANLVWQLGRDLLNMYIETEGKMIMQDKLEKERNDAKNAVEECVYEFRDKLCGPYEKFICEQEHEKFLRLLTETEDWLYEEGEDQAKQAYIDKLEELMKMGTPVKVRFQEAEERPKVLEELGQRLQHYAKIAADFRGKDEKYNHIDESEMKKVEKSVNEVMEWMNNVMNAQAKRSLDQDPVVRTHEIRAKVKELNNVCEPVVTQPKPKIESPKLERTPNGPNIDKKEDLEGKNNLGAEAPHQNGECHPNEKGSVNMDLD | Function: Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release (By similarity). Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities .
PTM: Phosphorylation on Ser-509 may be important for regulation of the HSPA8/HSC70 chaperone activity.
Sequence Mass (Da): 96407
Sequence Length: 858
Subcellular Location: Cytoplasm
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Q9S7U5 | MVKSTDGGGGSSSSSSVAPFLRKCYDMVDDSTTDSIISWSPSADNSFVILDTTVFSVQLLPKYFKHSNFSSFIRQLNIYGFRKVDADRWEFANDGFVRGQKDLLKNVIRRKNVQSSEQSKHESTSTTYAQEKSGLWKEVDILKGDKQVLAQELIKVRQYQEVTDTKMLHLEDRVQGMEESQQEMLSFLVMVMKNPSLLVQLLQPKEKNTWRKAGEGAKIVEEVTDEGESNSYGLPLVTYQPPSDNNGTAKSNSNDVNDFLRNADMLKFCLDENHVPLIIPDLYDDGAWEKLLLLSPSRKKTKKQENIVKKGKDDLTLEEEEEDGTMELDKSYMLKLISEEMEKPDDFEFGQLTPERSRNLEILTEQMELLASNE | Function: Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 42630
Sequence Length: 374
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain. AHA motifs are transcriptional activator elements.
Subcellular Location: Cytoplasm
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Q9LVW2 | MTAIPNVVDIESSSSSLCQETATETVTVERGSSDSSSKPDDVVLLIKEEEDDAVNLSLGFWKLHEIGLITPFLRKTFEIVDDKVTDPVVSWSPTRKSFIIWDSYEFSENLLPKYFKHKNFSSFIRQLNSYGFKKVDSDRWEFANEGFQGGKKHLLKNIKRRSKNTKCCNKEASTTTTETEVESLKEEQSPMRLEMLKLKQQQEESQHQMVTVQEKIHGVDTEQQHMLSFFAKLAKDQRFVERLVKKRKMKIQRELEAAEFVKKLKLLQDQETQKNLLDVEREFMAMAATEHNPEPDILVNNQSGNTRCQLNSEDLLVDGGSMDVNGRIEIE | Function: Seed-specific transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE). Seems to be specialized for the developmental expression of heat shock protein (HSP) genes during seed maturation. Activated by ABI3.
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 38146
Sequence Length: 331
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Nucleus
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Q10PR4 | MGSKKRSPQHPAAAAPPPAVGGGGGGEVSGDGGASTANGPVVPKPSEVAPFLTKVYDMVSDPATDNVISWAEGGGSFVIWDSHAFERDLHRHFKHSNFTSFIRQLNTYGFRKVHPDRWEWANEGFIMGQKHLLKTIKRRKKSSQESPSEIQKAPVKTAPGTENIEIGKYGGLEKEVETLKRDKALLMQQLVDLRHYQQTSNLEVQNLIERLQVMEQNQQQMMALLAIVVQNPSFLNQLVQQQQQQRRSNWWSPDGSKKRRFHALEQGPVTDQETSGRGAHIVEYLPPVPETSGQVNPVEGAICSANSQPVPSPAVATPMDMQTSNVADTLGSSEEPFADNSTLHEWDDNDMQLLFDDNLDPILPPFENDGQMGPPLSVQDYDFPQLEQDCLMEAQYNSNNPQYADVITEA | Function: Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 45466
Sequence Length: 410
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Cytoplasm
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Q96320 | MTAVTAAQRSVPAPFLSKTYQLVDDHSTDDVVSWNEEGTAFVVWKTAEFAKDLLPQYFKHNNFSSFIRQLNTYGFRKTVPDKWEFANDYFRRGGEDLLTDIRRRKSVIASTAGKCVVVGSPSESNSGGGDDHGSSSTSSPGSSKNPGSVENMVADLSGENEKLKRENNNLSSELAAAKKQRDELVTFLTGHLKVRPEQIDKMIKGGKFKPVESDEESECEGCDGGGGAEEGVGEGLKLFGVWLKGERKKRDRDEKNYVVSGSRMTEIKNVDFHAPLWKSSKVCN | Function: Transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 31328
Sequence Length: 284
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Nucleus
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Q67TP9 | MAAAEAAAAVGKQQQKGGGGRGGGGGGPAPFLTKTNQMVEESATDEVISWGKEGRSFVVWKPVEFARDLLPLHFKHCNFSSFVRQLNTYGFRKVVPDRWEFANGNFRRGEQGLLSGIRRRKATTPQSSKSCGSGVNVAFPPPLPPLPPEPSATTSSGNDRSSSSASSPPRADITSENEQLRKDNQTLTMELARARRHCEELLGFLSRFLDVRQLDLRLLMQEDMRAAAGGVGGEQRVQEHAREEKCVKLFGVLLDDTHGAATRKRARCEEAAASERPIKMIRIGEPWVSVPSSGPARCGGDN | Function: Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 32799
Sequence Length: 302
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Cytoplasm
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O22230 | MEDAGEHLRCNDNVNDEERLPLEFMIGNSTSTAELQPPPPFLVKTYKVVEDPTTDGVISWNEYGTGFVVWQPAEFARDLLPTLFKHCNFSSFVRQLNTYGFRKVTTIRWEFSNEMFRKGQRELMSNIRRRKSQHWSHNKSNHQVVPTTTMVNQEGHQRIGIDHHHEDQQSSATSSSFVYTALLDENKCLKNENELLSCELGKTKKKCKQLMELVERYRGEDEDATDESDDEEDEGLKLFGVKLE | Function: Transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 28308
Sequence Length: 244
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Cytoplasm
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Q9C635 | MAMMVENSYGGYGGGGGERIQLMVEGQGKAVPAPFLTKTYQLVDDPATDHVVSWGDDDTTFVVWRPPEFARDLLPNYFKHNNFSSFVRQLNTYGFRKIVPDRWEFANEFFKRGEKHLLCEIHRRKTSQMIPQQHSPFMSHHHAPPQIPFSGGSFFPLPPPRVTTPEEDHYWCDDSPPSRPRVIPQQIDTAAQVTALSEDNERLRRSNTVLMSELAHMKKLYNDIIYFVQNHVKPVAPSNNSSYLSSFLQKQQQQQPPTLDYYNTATVNATNLNALNSSPPTSQSSITVLEDDHTNHHDQSNMRKTKLFGVSLPSSKKRSHHFSDQTSKTRLVLDQSDLALNLMTASTR | Function: Transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 39615
Sequence Length: 348
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Cytoplasm
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Q9LV52 | MEDDNSNNNNNNNVIAPFIVKTYQMVNDPSTDWLITWGPAHNSFIVVDPLDFSQRILPAYFKHNNFSSFVRQLNTYGFRKVDPDRWEFANEHFLRGQKHLLNNIARRKHARGMYGQDLEDGEIVREIERLKEEQRELEAEIQRMNRRIEATEKRPEQMMAFLYKVVEDPDLLPRMMLEKERTKQQQQVSDKKKRRVTMSTVKSEEEEVEEDEGRVFRVMSSSTPSPSSTENLYRNHSPDGWIVPMTQGQFGSYETGLVAKSMLSNSTSSTSSSLTSTFSLPESVNGGGGGGCGSIQGERRYKETATFGGVVESNPPTTPPYPFSLFRGGF | Function: Transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 37714
Sequence Length: 330
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Nucleus
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Q5AQ33 | MIMNMTTDYRDPLLDLFGTESNSGNETSSPSDIPVINRSGTFNQQQFSPLLTQQSLYNTPNSGSTPNIFDPNYTQMQEEQTSPSSNKLQPEDPPRKKRNTRSQTKIHQQSEGDEYNSNDYKDSIDLDKPPVVEPSPPFFVESDTTPEFVIPTPTSEQQQQQHHELIAQDYQRSNNSNQFGNLTHYEPNLPPLPPLSESILPQTNTFHPLVLPHDPRHAITAGPANNSQQQQQQQQQDSSIPSDGISSKIQQLHAPSLSNNQSASQRKKKESSGPKTRPAFVMKIWSMVNDPANHEYIRWNDDGKTFQVFHREDFMKVILPKYFKHNNFASFVRQLNMYGWHKVQDVANGTLNQNSDKNGQDEIWQFENPNFIKDREDLLDKIVRNKSSSNQDDVSGVSFNGINNSANLSLILQELETIKMNQYVISEDLRRVRQDNKMLWQENYLNRERNQVQGRTLDKILKFLSVVYGNNANKILNGHGFADFNDSNNIMTQYRPSPMGSPLLSRPQTQPPPSNSRFARDNNQTAQPTYESPLSTSDTNNNNNNTFEYQQAVNRPRLMLTNRAHSRRPSMSRTKSTPEGSIEEIIRSYSNDKAAESNVNRMYEQLVGHQPGATTNNNNHSSSTAISAPSPRHSFLQELNLPGTPRNLDDLEKHINKEGQSIQQVQDWIDKLAQEQHEKQQQQQGNDDDDDFDVNEFLKDATTTPSSNVPNGGHYNNGNISFVGSPIAMTPGSNVSSNINDSDGNEKKSKKRSIEEVSDH | Function: DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription. With HSP90, is required for the modulation of the chaperone levels in response to growth temperature, rather than the activation of acute responses to sudden thermal transitions. Activated during infection and contributes to full virulence.
PTM: Activated by phosphorylation of at least Ser-570, Thr-574, Ser-576 and Thr-577 in response to heat shock. Additional unidentified residues are also phosphorylated in response to heat shock.
Sequence Mass (Da): 86197
Sequence Length: 760
Subcellular Location: Nucleus
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J9VHZ9 | MTTNLYAIAGPSKPTTPTSTPSPRSEPPSPLKSLTSLPTNPLNPQGTSTSNALTNQSSSTGIGISKPGLSVDENGEVMKVPAFLNKLYTMVSDPEVDDLIYWGENGDSFFVPNAELFGRELLPRWFKHSNFSSFVRQLNMYGFHKVPHLQSGALKNETPIELWEFANPYFKRGQPQLLTKVTRKNNRLSNSGVGSSSSLGGSGAGGGMNTRSASAAAASGSGSGQIQQAISQGHEAGNHSTSGKYLITDGTTPGSAPPSHTSAGPLIAPQTLDLSAINSGIAAIRQTQASIATDLRKLQASNEALWRQAYETQEKQRKHEETIDLIVSFLERLFGTEGEGLKGLKEAMRRGVGVRRDRDGREGRDSRDARFADDDDGGQKKRRRVGLDRMIEGGSGDGTGEHGEIESPSSDDRLVEIGSNSEYSIPSVKRTSSSSHPLSLGQLGSSRFTALPSEDPSPSGSGLGSTPYEGLRTTQASAHGAGADVNVTDPTLGMNHLSPLSDTDPLLPSSSNALAPYTSHPSFPSSNPNPSSAWAFNPSQPLLSPTSAVAAAHAYNLDPSLLQTTIGSLLQSPAVAQMFLKSLSASAQGQALTSHSHPHNPSLLNPNPNGNASTSASASAHDMNTEGLGTGSGTKDLDPTLALFSPLPSHSSLASQSNDLLKSYNDALTVGEGVDNLQESIDSLVRSMGLDLPNGGSSSVGVDVGDGSGVGTGTGEGDGEFNVDEFLQGLAKEGEGEEGEREVGGDGDASSSGAGAENGRKEDVIAQSGLK | Function: DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription . Promotes thermotolerance by transiently regulating a subset of genes . Induces expression of STI, SSA1, SSA2, HSP78 and KAR2 during the heat response .
PTM: Phosphorylated at high temperature.
Sequence Mass (Da): 80301
Sequence Length: 771
Subcellular Location: Nucleus
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P22813 | MSRSRSSAKAVQFKHESEEEEEDEEEQLPSRRMHSYGDAAAIGSGVPAFLAKLWRLVDDADTNRLICWTKDGQSFVIQNQAQFAKELLPLNYKHNNMASFIRQLNMYGFHKITSIDNGGLRFDRDEIEFSHPFFKRNSPFLLDQIKRKISNNKNGDDKGVLKPEAMSKILTDVKVMRGRQDNLDSRFSAMKQENEVLWREIASLRQKHAKQQQIVNKLIQFLITIVQPSRNMSGVKRHVQLMINNTPEIDRARTTSETESESGGGPVIHELREELLDEVMNPSPAGYTAASHYDQESVSPPAVERPRSNMSISSHNVDYSNQSVEDLLLQGNGTAGGNILVGGAASPMAQSVSQSPAQHDVYTVTEAPDSHVQEVPNSPPYYEEQNVLTTPMVREQEQQKRQQLKENNKLRRQAGDVILDAGDILVDSSSPKAQRTSIQHSTQPDVMVQPMIIKSEPENSSGLMDLMTPANDLYSVNFISEDMPTDIFEDALLPDGVEEAAKLDQQQKFGQSTVSSGKFASNFDVPTNSTLLDANQASTSKAAAKAQASEEEGMAVAKYSGAENGNNRDTNNSQLLRMASVDELHGHLESMQDELETLKDLLRGDGVAIDQNMLMGLFNDSDLMDNYGLSFPNDSISSEKKAPSGSELISYQPMYDLSDILDTDDGNNDQEASRRQMQTQSSVLNTPRHEL | Function: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 76933
Sequence Length: 691
Subcellular Location: Nucleus
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P22121 | MGHNDSVETMDEISNPNNILLPHDGTGLDATGISGSQEPYGMVDVLNPDSLKDDSNVDEPLIEDIVNPSLDPEGVVSAEPSNEVGTPLLQQPISLDHVITRPASAGGVYSIGNSSTSSAAKLSDGDLTNATDPLLNNAHGHGQPSSESQSHSNGYHKQGQSQQPLLSLNKRKLLAKAHVDKHHSKKKLSTTRARPAFVNKLWSMVNDKSNEKFIHWSTSGESIVVPNRERFVQEVLPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSMLSNNDSRWEFENENFKRGKEYLLENIVRQKSNTNILGGTTNAEVDIHILLNELETVKYNQLAIAEDLKRITKDNEMLWKENMMARERHQSQQQVLEKLLRFLSSVFGPNSAKTIGNGFQPDLIHELSDMQVNHMSNNNHNNTGNINPNAYHNETDDPMANVFGPLTPTDQGKVPLQDYKLRPRLLLKNRSMSSSSSSNLNQRQSPQNRIVGQSPPPQQQQQQQQQQGQPQGQQFSYPIQGGNQMMNQLGSPIGTQVGSPVGSQYGNQYGNQYSNQFGNQLQQQTSRPALHHGSNGEIRELTPSIVSSDSPDPAFFQDLQNNIDKQEESIQEIQDWITKLNPGPGEDGNTPIFPELNMPSYFANTGGSGQSEQPSDYGDSQIEELRNSRLHEPDRSFEEKNNGQKRRRAA | Function: DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription.
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 75420
Sequence Length: 677
Subcellular Location: Nucleus
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Q8YAC4 | MSDYLVKALAYDGMARVYAAVTTETIKEAQRRHDTWSVSSAALGRTMTGTLFLGAMQKEDQKITVKIEGDGPIGPIVADSNAQGQIRGYVTNPHVHFSELNEAGKLDVRRGVGTSGMLSVVKDLGFGENFTGQTPIVSGEIGEDFTYYLATSEQINSSVGVGVLVNPDDTIEAAGGFMLQLLPGATDEIIDEIEKNLMALPTVSRMIEAGETPESILAKLAGGEDKLQILEKIPVSFECNCSKERFGSAIISLGKEEIRSMIEEDHGAEAECHFCRNTYDFSEEELKTLYEEAK | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.
Sequence Mass (Da): 31915
Sequence Length: 294
Subcellular Location: Cytoplasm
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Q1H2B1 | MQISDHLHRFLFENTPVRGSIVHLDDSFQQSLQHHDFPQILRQALGELMAASALLAATLKLKGGALVLQVQGKGPLKLLVVECTSDLGIRATAKWSGELDGMSFSDMVSNGHFVITLDPRDGGQPYQGIVPVEGGSIAEILQSYMQRSEQIDTRMWLACDGKRAAGMLVQKMPDQPDAADPDAWNRIIMLADTVRDEELLDLSAVSLIKRLFNEEDVRLFKEQPIKFHCGCSRESVGNMLRMLGEEEVADILAEQHTIDINCDFCNAEYHFDEVDAEQLFTTEIVMPGNDVRH | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.
Sequence Mass (Da): 32692
Sequence Length: 293
Subcellular Location: Cytoplasm
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Q9JWC8 | MNQTAINRADVRTRFIFDDMPVRGLHVRLENVWQHIVKQKNYPAAIRRALGELLAAGVLLSGNLKNEGTLIVQVQGQGRLKMLVAEATSDRTVRATARWDETAEIADDESLGDLLGEGGVFVLTLQPKDGEPWQGVVPLEGDGIAQMLVNYMKRSEQLDTHIVLSASDEAAGGLLVQRLPEEVLDEEAWEHVSTLARTLTAEELAGLDAQHVLYRLFHETPPRVFEPETFEFSCTCSRGKVSDMLLMLGGEEVGGVVVEQGSIEVDCDFCHSKYVFDETDVNALFGEDVVGVAKGLPRHTVQ | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.
Sequence Mass (Da): 33265
Sequence Length: 302
Subcellular Location: Cytoplasm
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Q3J9G2 | MNNRDNLHRFLFEEAKIRGELVQLDASWRAVLACHDYPAVVQSQLGQALAATILLSATIKFKGSLILQTQSEGPLQTLVAQATHHRTLRGLARWDGDVPHGSLSETYGSGRLALTIQTEGKNPYQGIVSLEGVNLAEALQTYFSRSEQLRTRLWLVADEQQAVGLFLQELPSQQGHKTDWERIALLASTVTTQEMLSLPSTELLYRLFNEEQVRLFEPEPVSFRCGCSRGRIEQTLAALGREEMESILKEQGIIEVDCEFCNRHYNFDRVDMEQLFTEQVKAPVTSTRH | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.
Sequence Mass (Da): 32657
Sequence Length: 289
Subcellular Location: Cytoplasm
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P57115 | MTTILSVRLKNKVVIGGDGQATLGNTIMKSNVKKIRSLYHEKVIAGFAGGTADAFTLFEMFDKKLAMYQGQLQRAAIELAKDWRSDRMLRKLEALLAVADKKTSLIITGNGDVIQPEDDLIAIGSGGSYAQSSARALIENTHLDANQIVRKSLNIAANICIYTNHNFTIKELFSEK | Function: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Catalytic Activity: ATP-dependent cleavage of peptide bonds with broad specificity.
Sequence Mass (Da): 19317
Sequence Length: 176
Subcellular Location: Cytoplasm
EC: 3.4.25.2
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Q9ZDK9 | MSDNFALHGTTILCLKKKEEIIIAADGQVSHGNTVLKSTARKLRTIANNKIIVGFAGSTADGLALFEKLEIKIEQYNSNLLRSAVELAKDWRNDKYLRRLEAMMIVADRSHILILTGNGDVIEPENNVAAIGSGGLFALSAARALMSYENNLTAEEIALKSMNIAADLCVFSNHNIIMEKVV | Function: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Catalytic Activity: ATP-dependent cleavage of peptide bonds with broad specificity.
Sequence Mass (Da): 19873
Sequence Length: 182
Subcellular Location: Cytoplasm
EC: 3.4.25.2
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Q28222 | MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEADLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTRTIAYALDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTTWVEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETPGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPGVPQIEVTFEIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYALNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGGGGPGPGGFGAQGPKGGSGSGPTIEEVD | Function: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation.
PTM: In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and STUB1. The acetylated form and the non-acetylated form bind to HOPX and STUB1 respectively. Acetylation also protects cells against various types of cellular stress.
Sequence Mass (Da): 69920
Sequence Length: 638
Domain: The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins.
Subcellular Location: Cytoplasm
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